>WP_011914873.1 NCBI__GCF_000013785.1:WP_011914873.1
MTFDLASRLAARRAEHLYRRRPLLQSPQGPEVTVDGERLLAFSSNDYLGLANHPEVIAALQQGAATWGVGGGASHLVIGHSTPHHRLEEALAEFTGRPRALLFSTGYMANLAAVTALVGQGDTVLEDRLNHASLLDAGLLSGARFSRYLHNDASSLAKRLEKASGNTLVVTDGVFSMDGDLADLPALCAEAKRHGAWVMVDDAHGFGPLGATGGGIAEHFGLGIDEVPVLVGTLGKAFGTAGAFVAGSEELIETLIQFARPYIYTTSQPPAVACATLKSLELLRSEGWRREHLNRLVARFREGAARIGLTLMASPTPIQPVLVGSSERALRLSALLRERGILVGAIRPPTVPAGSARLRITLTAAHTDAQLERLLEALAECWALMPEECDDA
>biolip__1dj9A Crystal structure of 8-amino-7-oxonanoate synthase (or 7-keto- 8aminipelargonate or kapa synthase) complexed with plp and the product 8(s)-amino-7-oxonanonoate (or kapa). The enzyme of biotin biosynthetic pathway.
SWQEKINAALDARGAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGVSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLRQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVLHGNG
>PDB_1dje_A Crystal structure of the plp-bound form of 8-amino-7-oxonanoate synthase
SWQEKINAALDARGAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSG
YSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARL
LASPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGVS
GAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQ
PLIVGDNSRALQLAEKLRQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVLHGNG
>ecocyc__7KAPSYN-MONOMER 8-amino-7-oxononanoate synthase (EC 2.3.1.47) (Escherichia coli K-12 substr. MG1655)
MSWQEKINAALDARRAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGVSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLRQQGCWVTAIRPPTVPAGTARLRLTLTAAHEMQDIDRLLEVLHGNG
>PDB_2g6w_A Suicide inhibition of a-oxamine synthase: structures of the covalent adducts of 8-amino-7-oxonanoate synthase with trifluoroalanine
SWQEKINAALDARRAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSG
YSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARL
LASPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGVS
GAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQ
PLIVGDNSRALQLAEKLRQQGCWVTAIRPPTVPAGTARLRLTLTAAHEMQDIDRLLEVLHGNG
>ENA__BAB39457.1 KAPA synthase (Kurthia sp. 538-KA26)
MIWEKELEKIKEGGLYRQLQTVETMSDQGYAMVNGKKMMMFASNNYLGIANDQRLIEASVQATQRFGTGSTGSRLTTGNTIVHEKLEKRLAEFKQTDAAIVLNTGYMANIAALTTLVGSDDLILSDEMNHASIIDGCRLSRAETIIYRHADLLDLEMKLQINTRYRKRIIVTDGVFSMDGDIAPLPGIVELAKRYDALVMVDDAHATGVLGKDGRGTSEHFGLKGKIDIEMGTLSKAVGAEGGYIAGSRSLVDYVLNRARPFVFSTALSAGVVASALTAVDIIQSEPERRVRIRAMSQRLYNELTSLGYTVSGGETPILAIICGEPEQAMFLSKELHKHGIYAPAIRSPTVPLGTSRIRLTLMATHQEEQMNHVIDVFRTILTNRYK
>metacyc__MONOMER-14018 8-amino-7-oxononanoate synthase (EC 2.3.1.47) (Lysinibacillus sphaericus)
MNDRFRRELQVIEEQGLTRKLRLFSTGNESEVVMNGKKFLLFSSNNYLGLATDSRLKKKATEGISKYGTGAGGSRLTTGNFDIHEQLESEIADFKKTEAAIVFSSGYLANVGVISSVMKAGDTIFSDAWNHASIIDGCRLSKAKTIVYEHADMVDLERKLRQSHGDGLKFIVTDGVFSMDGDIAPLPKIVELAKEYKAYIMIDDAHATGVLGNDGCGTADYFGLKDEIDFTVGTLSKAIGAEGGFVSTSSIAKNYLLNNARSFIFQTALSPSAIEAAREGISIIQNEPERRKQLLKNAQYLRLKLEESGFVMKEGETPIISLIIGGSHEAMQFSAKLLDEGVFIPAIRPPTVPKGSSRLRITVMATHTIEQLDMVISKIKKIGKEMGIV
>SwissProt__Q5SHZ8 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase; AONS/AKB ligase; 7-keto-8-amino-pelargonic acid synthase; 7-KAP synthase; KAPA synthase; 8-amino-7-ketopelargonate synthase; Alpha-oxoamine synthase; Glycine acetyltransferase; EC 2.3.1.29; EC 2.3.1.47 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
MSLDLRARVREELERLKREGLYISPKVLEAPQEPVTRVEGREVVNLASNNYLGFANHPYLKEKARQYLEKWGAGSGAVRTIAGTFTYHVELEEALARFKGTESALVLQSGFTANQGVLGALLKEGDVVFSDELNHASIIDGLRLTKATRLVFRHADVAHLEELLKAHDTDGLKLIVTDGVFSMDGDIAPLDKIVPLAKKYKAVVYVDDAHGSGVLGEKGKGTVHHFGFHQDPDVVQVATLSKAWAGIGGYAAGARELKDLLINKARPFLFSTSHPPAVVGALLGALELIEKEPERVERLWENTRYFKRELARLGYDTLGSQTPITPVLFGEAPLAFEASRLLLEEGVFAVGIGFPTVPRGKARIRNIVTAAHTKEMLDKALEAYEKVGKRLGIIR
>biolip__3tqxA Structure of the 2-amino-3-ketobutyrate coenzyme a ligase (kbl) from coxiella burnetii
MQEILSQLNKEIEGLKKAGLYKSERIITSPQNAEIKVGEKEVLNFCANNYLGLADHPALIKTAQTVVEQYGFGMASVRFICGTQTIHKELEKDISEFLGTDDTILYSSCFDANGGLFETLLGPEDAIISDELNHASIIDGIRLCKAQRYRYKNNAMGDLEAKLKEADEKGARFKLIATDGVFSMDGIIADLKSICDLADKYNALVMVDDSHAVGFIGENGRGTPEYCGVADRVDILTGTLGKALGGASGGYTSGHKEIIEWLRNRSRPYLFSNTVAPVIVATSLKVLELLKTEGPQLRKQLQENSRYFRAGMEKLGFQLVPGNHPIIPVMLGDAQLATNMADHLLQEGIYVVGFSYPVVPMGKARIRVQMSAVHTQQQLDRAIEAFGQVGKKLGAI
>biolip__7poaA An irreversible, promiscuous and highly thermostable claisen- condensation biocatalyst drives the synthesis of substituted pyrroles
GAMGSLDLRARVREELERLKREGLYISPKVLEAPQEPVTRVEGREVVNLASNNYLGFANHPYLKEKARQYLEKWGAGSGAVRTIAGTFTYHVELEEALARFKGTESALVLQSGFTANQGVLGALLKEGDVVFSDELNHASIIDGLRLTKATRLVFRHADVAHLEELLKAHDTDGLKLIVTDGVFSMDGDIAPLDKIVPLAKKYKAVVYVDDAHGSGVLGEKGKGTVHHFGFHQDPDVVQVATLSKAWAGIGGYAAGARELKDLLINKARPFLFSTSHPPAVVGALLGALELIEKEPERVERLWENTRYFKRELARLGYDTLGSQTPITPVLFGEAPLAFEASRLLLEEGVFAVGIGFPTVPRGKARIRNIVTAAHTKEMLDKALEAYEKVGKRLGIIR
>reanno__ANA3_7026975 2-amino-3-ketobutyrate coenzyme A ligase (EC 2.3.1.29) (Shewanella sp. ANA-3)
MASTSFYAQINQQLADVKAEGLYKSERVIASPQQTAIQVNHQEVVNFCANNYLGLANHPELIKAAQQGLDSHGFGMASVRFICGTQDIHKQLEASLSEFLGMEDTILYSSCFDANAGLFETLLDAEDAIISDALNHASIIDGVRLCKAKRFRYANNDMADLETQLIAAKAAGARNILIATDGVFSMDGVIANLQGVCDLADKYGALVMVDDSHAVGFVGLNGRGSHEHCGVMGRVDIITGTLGKALGGASGGFTSGKKEVIDWLRQRSRPYLFSNSLAPSIVTASIHVLEMLKSGQALREAVWENSRYFREKMSAAGFTLGGADHAIIPVMIGDAKLASDFANRLLAEHIYVIGFSFPVVPKGQARIRTQMSAAHTREQLDKAIEAFTRIAKEMAII
>SwissProt__A7BFV6 Serine palmitoyltransferase; SPT; EC 2.3.1.50 (Sphingobacterium multivorum)
MSKGKLGEKISQFKIVEELKAKGLYAYFRPIQSKQDTEVKIDGRRVLMFGSNSYLGLTTDTRIIKAAQDALEKYGTGCAGSRFLNGTLDIHVELEEKLSAYVGKEAAILFSTGFQSNLGPLSCLMGRNDYILLDERDHASIIDGSRLSFSKVIKYGHNNMEDLRAKLSRLPEDSAKLICTDGIFSMEGDIVNLPELTSIANEFDAAVMVDDAHSLGVIGHKGAGTASHFGLNDDVDLIMGTFSKSLASLGGFVAGDADVIDFLKHNARSVMFSASMTPASVASTLKALEIIQNEPEHIEKLWKNTDYAKAQLLDHGFDLGATESPILPIFIRSNEKTFWVTKMLQDDGVFVNPVVSPAVPAEESLIRFSLMATHTYDQIDEAIEKMVKVFKQAEVETLI
>biolip__8guhA Serine palmitoyltransferase from sphingobacterium multivorum complexed with tris
SKGKLGEKISQFKIVEELKAKGLYAYFRPIQSKQDTEVKIDGRRVLMFGSNSYLGLTTDTRIIKAAQDALEKYGTGCAGSRFLNGTLDIHVELEEKLSAYVGKEAAILFSTGFQSNLGPLSCLMGRNDYILLDERDHASIIDGSRLSFSKVIKYGHNNMEDLRAKLSRLPEDSAKLICTDGIFSMEGDIVNLPELTSIANEFDAAVMVDDAHSLGVIGHKGAGTASHFGLNDDVDLIMGTFSKSLASLGGFVAGDADVIDFLKHNARSVMFSASMTPASVASTLKALEIIQNEPEHIEKLWKNTDYAKAQLLDHGFDLGATESPILPIFIRSNEKTFWVTKMLQDDGVFVNPVVSPAVPAEESLIRFSLMATHTYDQIDEAIEKMVKVFKQAEV
>SwissProt__A7BFV7 Serine palmitoyltransferase; SPT; EC 2.3.1.50 (Sphingobacterium spiritivorum (Flavobacterium spiritivorum))
MSKGKLSERISHFNIVEELKSKGLYAYFRPIQSKQDTEVMIDGKRVLMFGSNSYLGLTIDPRIIEAAQDALSKYGTGCAGSRFLNGTLDIHIELEHKLSQLVGKEASILFSTGFQSNLGPISCLMGRNDYILLDERDHASIIDGSRLSFSKVIKYGHNDMDDLRAKLSRLPSESAKLIVTDGIFSMEGDIVNLPEMVKIADEYDAALMVDDAHSLGVIGEHGAGTASHFGLTDKVDLIMGTFSKSLASLGGFVAGDADVIDYLKHNARSVMFSASMTPASVASTLKALEIMISEPEHMENLWKNTNYAKQQLLESGFDLGATESPILPIFIRNNEKTFWVTKMLQDDGVFVNPVVSPAVPSEESLIRFSLMATHTFDQIDEAVEKMVRVFKQAEIESLI
>biolip__7v58B Structural insights into the substrate selectivity of acyl-coa transferase
NIMSSAFYQQIQQQIEEVKAEGLYKSERIITSQQQAAVKIASGEEVLNFCANNYLGLANHPALIEAGKAGMDEHGFGMASVRFICGTQDIHKELEQKLSTFLGKEDTILYTSCFDANAGLFETILDKEDAIISDALNHASIIDGVRLCKAMRFRYSNNNMTELEEQLIAAKDAGARNILIVTDGVFSMDGVVANLPAICDLAEKYGALTMVDDSHAVGFMGKTGAGTHEYHDVVDRIDIITGTLGKAMGGASGGYTSGKKEVIEWLRQRSRPYLFSNSVAPAIVSASIRVLDLLQESGDLRDRLWENATHFRTRMSEAGFTLAGADHAIIPIMLGDAKVAAEFAERALEKGIYVIGFSFPVVPKGQARIRTQMSAAHSREQLDKAIDAFIEVGRDMEIIK
>PDB_8iyt_A Crystal structure of serine palmitoyltransferase complexed with d- methylserine
SKGKLGEKISQFKIVEELKAKGLYAYFRPIQSKQDTEVKIDGRRVLMFGSNSYLGLTTDTRIIKAAQDALEKYGTGCAGS
RFLNGTLDIHVELEEKLSAYVGKEAAILFSTGFQSNLGPLSCLMGRNDYILLDERDHASIIDGSRLSFSKVIKYGHNNME
DLRAKLSRLPEDSAKLICTDGIFSMEGDIVNLPELTSIANEFDAAVMVDDAHSLGVIGHKGAGTASHFGLNDDVDLIMGT
FSKSLASLGGFVAGDADVIDFLKHNARSVMFSASMTPASVASTLKALEIIQNEPEHIEKLWKNTDYAKAQLLDHGFDLGA
TESPILPIFIRSNEKTFWVTKMLQDDGVFVNPVVSPAVPAEESLIRFSLMATHTYDQIDEAIEKMVKVFKQAEV
>PDB_8h29_A Serine palmitoyltransferase from sphingobacterium multivorum complexed with l-threonine
SKGKLGEKISQFKIVEELKAKGLYAYFRPIQSKQDTEVKIDGRRVLMFGSNSYLGLTTDTRIIKAAQDALEKYGTGCAGS
RFLNGTLDIHVELEEKLSAYVGKEAAILFSTGFQSNLGPLSCLMGRNDYILLDERDHASIIDGSRLSFSKVIKYGHNNME
DLRAKLSRLPEDSAKLICTDGIFSMEGDIVNLPELTSIANEFDAAVMVDDAHSLGVIGHKGAGTASHFGLNDDVDLIMGT
FSKSLASLGGFVAGDADVIDFLKHNARSVMFSASMTPASVASTLKALEIIQNEPEHIEKLWKNTDYAKAQLLDHGFDLGA
TESPILPIFIRSNEKTFWVTKMLQDDGVFVNPVVSPAVPAEESLIRFSLMATHTYDQIDEAIEKMVKVFKQAEV
>PDB_8h21_A Serine palmitoyltransferase from sphingobacterium multivorum complexed with l-alanine
SKGKLGEKISQFKIVEELKAKGLYAYFRPIQSKQDTEVKIDGRRVLMFGSNSYLGLTTDTRIIKAAQDALEKYGTGCAGS
RFLNGTLDIHVELEEKLSAYVGKEAAILFSTGFQSNLGPLSCLMGRNDYILLDERDHASIIDGSRLSFSKVIKYGHNNME
DLRAKLSRLPEDSAKLICTDGIFSMEGDIVNLPELTSIANEFDAAVMVDDAHSLGVIGHKGAGTASHFGLNDDVDLIMGT
FSKSLASLGGFVAGDADVIDFLKHNARSVMFSASMTPASVASTLKALEIIQNEPEHIEKLWKNTDYAKAQLLDHGFDLGA
TESPILPIFIRSNEKTFWVTKMLQDDGVFVNPVVSPAVPAEESLIRFSLMATHTYDQIDEAIEKMVKVFKQAEV
>PDB_8h20_A Serine palmitoyltransferase from sphingobacterium multivorum complexed with glycine
SKGKLGEKISQFKIVEELKAKGLYAYFRPIQSKQDTEVKIDGRRVLMFGSNSYLGLTTDTRIIKAAQDALEKYGTGCAGS
RFLNGTLDIHVELEEKLSAYVGKEAAILFSTGFQSNLGPLSCLMGRNDYILLDERDHASIIDGSRLSFSKVIKYGHNNME
DLRAKLSRLPEDSAKLICTDGIFSMEGDIVNLPELTSIANEFDAAVMVDDAHSLGVIGHKGAGTASHFGLNDDVDLIMGT
FSKSLASLGGFVAGDADVIDFLKHNARSVMFSASMTPASVASTLKALEIIQNEPEHIEKLWKNTDYAKAQLLDHGFDLGA
TESPILPIFIRSNEKTFWVTKMLQDDGVFVNPVVSPAVPAEESLIRFSLMATHTYDQIDEAIEKMVKVFKQAEV
>PDB_8h1y_A Serine palmitoyltransferase from sphingobacterium multivorum complexed with l-homoserine
SKGKLGEKISQFKIVEELKAKGLYAYFRPIQSKQDTEVKIDGRRVLMFGSNSYLGLTTDTRIIKAAQDALEKYGTGCAGS
RFLNGTLDIHVELEEKLSAYVGKEAAILFSTGFQSNLGPLSCLMGRNDYILLDERDHASIIDGSRLSFSKVIKYGHNNME
DLRAKLSRLPEDSAKLICTDGIFSMEGDIVNLPELTSIANEFDAAVMVDDAHSLGVIGHKGAGTASHFGLNDDVDLIMGT
FSKSLASLGGFVAGDADVIDFLKHNARSVMFSASMTPASVASTLKALEIIQNEPEHIEKLWKNTDYAKAQLLDHGFDLGA
TESPILPIFIRSNEKTFWVTKMLQDDGVFVNPVVSPAVPAEESLIRFSLMATHTYDQIDEAIEKMVKVFKQAEV
>PDB_8h1q_A Serine palmitoyltransferase from sphingobacterium multivorum complexed with l-serine
SKGKLGEKISQFKIVEELKAKGLYAYFRPIQSKQDTEVKIDGRRVLMFGSNSYLGLTTDTRIIKAAQDALEKYGTGCAGS
RFLNGTLDIHVELEEKLSAYVGKEAAILFSTGFQSNLGPLSCLMGRNDYILLDERDHASIIDGSRLSFSKVIKYGHNNME
DLRAKLSRLPEDSAKLICTDGIFSMEGDIVNLPELTSIANEFDAAVMVDDAHSLGVIGHKGAGTASHFGLNDDVDLIMGT
FSKSLASLGGFVAGDADVIDFLKHNARSVMFSASMTPASVASTLKALEIIQNEPEHIEKLWKNTDYAKAQLLDHGFDLGA
TESPILPIFIRSNEKTFWVTKMLQDDGVFVNPVVSPAVPAEESLIRFSLMATHTYDQIDEAIEKMVKVFKQAEV
>PDB_3a2b_A Crystal structure of serine palmitoyltransferase from sphingobacterium multivorum with substrate l-serine
SKGKLGEKISQFKIVEELKAKGLYAYFRPIQSKQDTEVKIDGRRVLMFGSNSYLGLTTDTRIIKAAQDALEKYGTGCAGS
RFLNGTLDIHVELEEKLSAYVGKEAAILFSTGFQSNLGPLSCLMGRNDYILLDERDHASIIDGSRLSFSKVIKYGHNNME
DLRAKLSRLPEDSAKLICTDGIFSMEGDIVNLPELTSIANEFDAAVMVDDAHSLGVIGHKGAGTASHFGLNDDVDLIMGT
FSKSLASLGGFVAGDADVIDFLKHNARSVMFSASMTPASVASTLKALEIIQNEPEHIEKLWKNTDYAKAQLLDHGFDLGA
TESPILPIFIRSNEKTFWVTKMLQDDGVFVNPVVSPAVPAEESLIRFSLMATHTYDQIDEAIEKMVKVFKQA
>reanno__Koxy_BWI76_RS27255 2-amino-3-ketobutyrate coenzyme A ligase (EC 2.3.1.29) (Klebsiella michiganensis M5al)
MRGDFYKQLTNDLDTARAEGLFKEERIITSAQQADITVGGSQVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGTQDSHKALEKKLADFLGMEDAILYSSCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRFRYANNDMVELEARLKEARDAGARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGSELRDRLWSNARLFREKMTAAGFILAGADHAIIPVMLGEATVAQEFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFTRIGKQLGVIA
>biolip__1fc4A 2-amino-3-ketobutyrate coa ligase
GSHMRGEFYQQLTNDLETARAEGLFKEERIITSAQQADITVADGSHVINFCANNYLGLANHPDLIAAAKAGMDSHGFGMASVRFICGTQDSHKELEQKLAAFLGMEDAILYSSCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMQELEARLKEAREAGARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGSELRDRLWANARQFREQMSAAGFTLAGADHAIIPVMLGDAVVAQKFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQITRAVEAFTRIGKQLGVIA
>ecocyc__AKBLIG-MONOMER 2-amino-3-ketobutyrate CoA ligase (EC 2.3.1.29) (Escherichia coli K-12 substr. MG1655)
MRGEFYQQLTNDLETARAEGLFKEERIITSAQQADITVADGSHVINFCANNYLGLANHPDLIAAAKAGMDSHGFGMASVRFICGTQDSHKELEQKLAAFLGMEDAILYSSCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMQELEARLKEAREAGARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGSELRDRLWANARQFREQMSAAGFTLAGADHAIIPVMLGDAVVAQKFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQITRAVEAFTRIGKQLGVIA
>metacyc__BSU30220-MONOMER 8-amino-7-oxononanoate synthase (pimeloyl-CoA-dependent) (EC 2.3.1.47) (Bacillus subtilis (strain 168))
MKIDSWLNERLDRMKEAGVHRNLRSMDGAPVPERNIDGENQTVWSSNNYLGLASDRRLIDAAQTALQQFGTGSSGSRLTTGNSVWHEKLEKKIASFKLTEAALLFSSGYLANVGVLSSLPEKEDVILSDQLNHASMIDGCRLSKADTVVYRHIDMNDLENKLNETQRYQRRFIVTDGVFSMDGTIAPLDQIISLAKRYHAFVVVDDAHATGVLGDSGQGTSEYFGVCPDIVIGTLSKAVGAEGGFAAGSAVFIDFLLNHARTFIFQTAIPPASCAAAHEAFNIIEASREKRQLLFSYISMIRTSLKNMGYVVKGDHTPIIPVVIGDAHKTVLFAEKLQGKGIYAPAIRPPTVAPGESRIRITITSDHSMGDIDHLLQTFHSIGKELHII
>ENA__BAB39461.1 KAPA synthase-II (Kurthia sp. 538-KA26)
MHSEKQLPCWEEKIKKELAYLEEISQKRELVSTEFAEQPWLMINGCKMLNLASNNYLGYAGDERLKKAMVDAVHTYGAGATASRLIIGNHPLYEQAEQALVNWKKAEAGLIINSGYNANLGIISTLLSRNDIIYSDKLNHASIVDGALLSRAKHLRYRHNDLDHLEALLKKSSMEARKLIVTDTVFSMDGDFAYLEDLVRLKERYNAMLMTDEAHGSGIYGKNGEGYAGHLHLQNKIDIQMGTFSKALGSFGAYVVGKKWLIDYLKNRMRGFIYSTALPPAILGAMKTAIELVQQEPERRSLLQTHSEHFREELTYYGFNICGSRSQIVPIVIGENEKAMEFATRLQKEGIAAIAVRPPTVPENEARIRFTVTALHDKKDLDWAVEKVSIIGKEMGVI
>metacyc__HS01980-MONOMER 2-amino-3-ketobutyrate coenzyme A ligase (EC 2.3.1.29) (Homo sapiens)
MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGIRGAGTWKSERVITSRQGPHIRVDGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
>reanno__Phaeo_GFF3380 2-amino-3-ketobutyrate coenzyme A ligase (EC 2.3.1.29) (Phaeobacter inhibens BS107)
MSTDFLTDISKTLEEIKADGLYKRERMITSPQGGEIRVGDAAVINLCANNYLGLADHPDLIAAARGVMDDKGFGMASVRFICGTQDIHRELEQRLAKFLGKDDAILFAACFDANGGLFEPLLGPEDAIISDSLNHASIIDGIRLCKAKRYRYLNSDMNDLEAWLKQAREDGARHIMIATDGVFSMDGYLAKLPEIRALADKYDAIVMVDDCHATGFMGATGAGTPEHFGVDVDIVTGTLGKALGGAIGGYIAGPQPVIDLLRQRARPYLFSNSLPPSIVAAGLEAIRLVEEGNGLRAQLFENAKYWRAGLEKLGFDLLPGEHPIIPVMLGEAQLAQDMASRLFDEGVYVSGFFFPVVPRGQARIRTQMNAALTRDELDRALAAFGKVGKELGILS
>SwissProt__A7BFV8 Serine palmitoyltransferase; SPT; EC 2.3.1.50 (Bacteriovorax stolpii (Bdellovibrio stolpii))
MKHNLQDNLQGEQMANTNSNGGKKPFSDAKIIERANLLRDNDLYFFFRAIEETEASTVTVKGKKQIMIGSNNYLGLTHHPAVKEAAIKAVEKYGTGCTGSRFLNGNLNIHEELDEKLAAYLGHEKAIVFSTGMQANLGALSAICGPKDLMLFDSENHASIIDASRLSLGTTFKYKHNDMASLEELLESNMSRFNRVIIVADGVFSMTGDILRLPEVVKLAKKYGAYVYVDDAHGLGVMGPQGRGTMAHFDVTKDVDFNMGTFSKSFASIGGVISGSKDAIDYVRHSARSFMFSASMPPAAVATVSACIDVVQNDETILNNLWSNVEFMRNGFKELGFFTYGSQTPIIPLFIGDDMKALKMTKWLESKGVFCTPVLPPAVPKGETLIRTSYMASHNREDLSTVLEVFAEAKKIFDIPNHLH
>SwissProt__Q0P5L8 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial; AKB ligase; Aminoacetone synthase; Glycine acetyltransferase; EC 2.3.1.29 (Bos taurus (Bovine))
MWAGRVLHAALSRAPRESRAQSALAQLRGILEEELESIRGAGTWKSERVITSRQGPHIHVDGAPGGIINFCANNYLGLSSHPEVIQAGLRTLKEFGAGLSSVRFICGTQSIHKDLEAKIARFHQREDAILYPSCFDANTGLFEALLTSEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICRLASQYGALVFVDESHATGFLGATGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGALVSLLRQRARPYLFSNSLPPAAVGCASKALDLLMESNAIVQSMAAKTLRFRSQMEAAGFTISGANHPICPVMLGDARLALNIADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
>SwissProt__O88986 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial; AKB ligase; Aminoacetone synthase; Glycine acetyltransferase; EC 2.3.1.29 (Mus musculus (Mouse))
MWASFMWHGALSPGRRAHSALAQLRCILDSELEGIRGAGTWKSERVITSRQGPSIRVDGISGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEAQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
>SwissProt__A7LXM2 Serine palmitoyltransferase; SPT; EC 2.3.1.50 (Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153))
MGLLQEKLAKYDLPQKFMAQGVYPYFREIEGKQGTEVEMGGHEVLMFGSNAYTGLTGDERVIEAGIKAMHKYGSGCAGSRFLNGTLDLHVQLEKELAAFVGKDEALCFSTGFTVNSGVIPALTDRNDYIICDDRDHASIVDGRRLSFSQQLKYKHNDMADLEKQLQKCNPDSVKLIIVDGVFSMEGDLANLPEIVRLKHKYNATIMVDEAHGLGVFGKQGRGVCDHFGLTHEVDLIMGTFSKSLASIGGFIAADSSIINWLRHNARTYIFSASNTPAATASALEALHIIQDEPERLEALWEATNYALKRFREAGFEIGATESPIIPLYVRDTEKTFMVTKLAFDEGVFINPVIPPACAPQDTLVRVALMATHTKDQIDRAVEKLVKAFKALDLL
>reanno__Cup4G11_RR42_RS28295 2-amino-3-ketobutyrate coenzyme A ligase (EC 2.3.1.29) (Cupriavidus basilensis FW507-4G11)
MPTTDAFYAAIRQELESIEQAGLFKTERVIASPQGSLIRTTDGKEVINLCANNYLGLSSHPEVVEAAHRALGERGFGLSSVRFICGTQDLHKSLEARLASFLGTEDTILYGSAFDANGGLFETLLGSDDAVISDELNHASIIDGIRLCKAKRFRYKNNDLEDLREQLKAADAAGARFKLVFTDGVFSMDGTIARLDEIREICDEFGALLGIDECHATGFLGQRGRGSHEHRGIFGKVDIITGTLGKALGGASGGFTSGRKEVVALLRQRSRPYLFSNTVAPCIVGATLKVLDLLEADTTLRDKLERNARYFRGKLGTLGFDVKPGDHPIIPVMVYDAEKAQRLSRRLLELGVYVIGFFYPVVPRGQARIRVQISALHDSAELDQALEAFEIAGKELGIIQ
>SwissProt__Q5W264 4-hydroxy-2,2'-bipyrrole-5-methanol synthase PigH; HBM synthase; Aminotransferase PigH; EC 2.3.2.- (Serratia sp. (strain ATCC 39006) (Prodigiosinella confusarubida))
MNDVTTETYETLKQSVLHTFAQLTGYNVSELSLTSHLENDLGVDSIALAEIAVSLSRQFQLNTPLLIQDINTIKDALDGILQREFQLSEKVEPAAIALSGDADLWLGNLVRQIFASHSGYDVNALALDAEIESDLGIDSVSVASAQGELFNTLQLNSETIIANCNTLSALKQCLAARLVQEKGQDWFEQRGRGQSDSAIDHDADTTAEVTPPTATPVAINAEIGDPRTMRDFVGIEHPDIFHKAREFHLFYQDKKKRQLYFYGMPLETPCKNRAVMFDEATGQHREFLMFGSNSYLGLSNHPEIIHAIQDAASLYGATNTGCRIIAGSNVLHLELERKLAKLKGRDDCIVYPSGYSANLGCISALTSRHDLVFTDAINHMSIQDGCKLAGAQRKIYNHSLTSLEKSLAKYADHPGGKLIVTDGVFSMHGDIVDLPRLMKLAERYGARVLVDDAHSTGVLGKTGAGTSEHFNMKGQVDLELGTMSKALSGLGGYVCGDGDVVEYLRFYSNSYVFAATIPAPVAAGVIASIDVMLREPERLAKLWDNIYYFRTRLLNAGFDLENSDSAIIPIVVGDDAKTLFFGRAVRARGMFCQTVVFPGVSVGDARLRISITSEHTREDLDEAYAILVASALEVGVPVNASAHQEENASVAEA
>SwissProt__Q8A9E5 Serine palmitoyltransferase; SPT; BtSPT; EC 2.3.1.50 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50))
MGLLQEKLAKYDLPQKFMAQGVYPYFREIEGKQGTEVEMGGQHVLMFGSNAYTGLTGDERVIEAGIKAMRKYGSGCAGSRFLNGTLDLHVQLEKELAAFVGKDEALCFSTGFTVNSGVISCLTDRNDYIICDDRDHASIVDGRRLSFSQQLKYKHNDMADLEKQLQKCNPDSVKLIIVDGVFSMEGDLANLPEIVRLKHKYNATIMVDEAHGLGVFGKQGRGVCDHFGLTHEVDLIMGTFSKSLASIGGFIAADSSIINWLRHNARTYIFSASNTPAATAAALEALHIIQNEPERLNALWEATNYALRRFREAGFEIGATESPIIPLYVRDTEKTFMVTKLAFDEGVFINPVIPPACAPQDTLVRVALMATHTKEQIDSAVEKLVKAFKALDLL
>metacyc__MONOMER-18832 PigH polyketide synthase (Serratia marcescens)
MSVHAVDSAANAHEAVRQSVLHTFARLTEYEPSALALTSHLENDLGVDSIALAEIAMVLNRQFQLNTPLAIQEIKTIQDALDGILQRGFTLPTPNAAAQPAPQTPQAWLSALVRQVFATHSGYEVRDLSPDAAIEGDLGIDSVAVVMARNELLKTLGLDDNAALAECRTLAELEHNLAARLVQEQGEAWFSRFGQHTTASAAPQPTKAPASPDARDELGDPRTMRDFVGIEHPDLFHKTREFGAFYRDKKQRQLYWYGMPLETPCKNRAVMFDEVTGKSREFLMFGSNSYLGLSNHPEVIHAIQDAAGLYGATNTGCRIIAGSNVLHLELERKLAKLKGREDCIVYPSGYSANLGCISALTSRHDLVFTDAINHMSIQDGCKLAGAQRKIYDHSLTSLEKSLAKYADHPGGKLIVTDGVFSMHGDIVDLPRLMKLAERYGARVLVDDAHATGVLGKTGSGTAEHFNMKGQVDLELGTMSKALSGLGGFVCADGEVVEYLRFYSNSYVFAATIPAAVAAGVIASIDVMLREPERLTKLWDNIYYFRTLLLNAGFDLEHSDSAIIPVVVGDDAKTLLFGRAVRARGLFCQTVVFPGVSVGDARLRISVTSEHTREDLDEANAILVAAALETGVPVNGDVRREERARATEV
>SwissProt__A0A0H3C7E9 Serine palmitoyltransferase; EC 2.3.1.50 (Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus))
MGLFDKHLAYRDAYKAIQDVGANPFKVRFDAVHSPTEGVVDGRPTILLGTNNYLGLTFDEQAIAASVKAVQERGTGTTGSRIANGSFESHVELEQELAKFYGRKHAMVFTTGYQANLGVLSTLVGRGDHLILDADSHASIYDGSRLGHAEVIRFRHNDPEDLAKRLRRLGDAPGERLIVVEGIYSMIGDVAPLKEIAAVKREMGGYLLVDEAHSMGVLGATGRGLAEAAGVEEDVDFIVGTFSKSLGAIGGFCVSDHDDFDVMRVICRPYMFTASLPPAVAASTVTALRRMIEQPELRDRLNRNAKRLYDGLTAMGFLTGPSASPIVAATMPDQERAIAMWNGLLQAGVYLNLALPPATPDSRPLLRASVSAAHTDEQIDAVLKTYGEIGAALGVIEPLKRARA
>biolip__2x8uA Sphingomonas wittichii serine palmitoyltransferase
ADLLSKFDPLIAEREALLATGVRDPYAIVMDKVLSPTEAMINGRKTILLGTYNYMGMTFDPDVIAAGKQALDEFGSGTTGSRVLNGTYQGHKACEDALKEFYGTEHAIVFSTGYQANLGMISTLAGKGDYIILDADSHASIYDGCWLGDAEIVRFRHNSVEDLDKRLGRLPAEAGKLVVLEGVYSMMGDIAPLQEMVAVSKKHGAMILVDEAHGMGFFGEHGRGVFEEAGVEADVDFVVGTFSKSVGTVGGFCVSNHPKFEVLRLVCRPYVFTASLPPSVVATAATSIRKLMHAGDKRAHLWKNSRRLHQGLRDMGYKLGTETAQSAIIAVILTDMAQAVALWQGLLEAGLYVNTARPPATPAGMFLLRCSLCAEHSDEQVEQILGMFESAGRATGVIP
>SwissProt__Q8GW43 8-amino-7-oxononanoate synthase; AONS; 7-keto-8-amino-pelargonic acid synthase; 7-KAP synthase; KAPA synthase; 8-amino-7-ketopelargonate synthase; Biotin synthase 4; Biotin synthase F; AtbioF; EC 2.3.1.47 (Arabidopsis thaliana (Mouse-ear cress))
MADHSWDKTVEEAVNVLESRQILRSLRPICMSRQNEEEIVKSRANGGDGYEVFDGLCQWDRTSVEVSVSIPTFQKWLHDEPSNGEEIFSGDALAECRKGRFKKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNHASIIDGVRLAERQGNVEVFVYRHCDMYHLNSLLSNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKELSGVDISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTATHIPSFLFPKL
>biolip__7bxqA 2-amino-3-ketobutyrate coa ligase from cupriavidus necator l-threonine binding form
MSNAEAFYASIRTELESIRAAGLFKNERVIATPQGARVRTTDGREVINLCANNYLGLSSHPQVIEAAHEALRTHGFGLSSVRFICGTQDLHKTLEARLSAFLGTEDTILYGSAFDANGGLFETLLGAEDAVISDALNHASIIDGVRLSKARRYRYQHNDMDDLRVQLEQARADGARYTLVFSDGVFSMDGTVARLDEMRAICDEYGALLGIDECHATGFMGQRGRGTHEARGVFGKIDIITGTLGAALGGASGGFTSARKEVVALLRQRSRPYLFSNTVAPAIVGASIAVLDILEASTELRDRLEGNTRFFRAGLDRLGFDVKAGDHPIIPIMVYDADKAQQLAQRLLELGVYVVGFFYPVVPKGQARIRVQMSALHDEAALQAALDAFGQAGRELGLI
>PDB_7bxs_A 2-amino-3-ketobutyrate coa ligase from cupriavidus necator glycine binding form
MSNAEAFYASIRTELESIRAAGLFKNERVIATPQGARVRTTDGREVINLCANNYLGLSSHPQVIEAAHEALRTHGFGLSS
VRFICGTQDLHKTLEARLSAFLGTEDTILYGSAFDANGGLFETLLGAEDAVISDALNHASIIDGVRLSKARRYRYQHNDM
DDLRVQLEQARADGARYTLVFSDGVFSMDGTVARLDEMRAICDEYGALLGIDECHATGFMGQRGRGTHEARGVFGKIDII
TGTLGAALGGASGGFTSARKEVVALLRQRSRPYLFSNTVAPAIVGASIAVLDILEASTELRDRLEGNTRFFRAGLDRLGF
DVKAGDHPIIPIMVYDADKAQQLAQRLLELGVYVVGFFYPVVPKGQARIRVQMSALHDEAALQAALDAFGQAGRELGLI
>PDB_7bxr_A 2-amino-3-ketobutyrate coa ligase from cupriavidus necator 3- hydroxynorvaline binding form
MSNAEAFYASIRTELESIRAAGLFKNERVIATPQGARVRTTDGREVINLCANNYLGLSSHPQVIEAAHEALRTHGFGLSS
VRFICGTQDLHKTLEARLSAFLGTEDTILYGSAFDANGGLFETLLGAEDAVISDALNHASIIDGVRLSKARRYRYQHNDM
DDLRVQLEQARADGARYTLVFSDGVFSMDGTVARLDEMRAICDEYGALLGIDECHATGFMGQRGRGTHEARGVFGKIDII
TGTLGAALGGASGGFTSARKEVVALLRQRSRPYLFSNTVAPAIVGASIAVLDILEASTELRDRLEGNTRFFRAGLDRLGF
DVKAGDHPIIPIMVYDADKAQQLAQRLLELGVYVVGFFYPVVPKGQARIRVQMSALHDEAALQAALDAFGQAGRELGLI
>BRENDA__Q9A8J8 5-aminolevulinate synthase (EC 2.3.1.37) (Caulobacter vibrioides)
MDYKAAFRSAVEQIREEGRYRVFADLKRQRGQFPRATWTRQDGSEHEVVVWCSNDYLGQGQNPVVLEAMKAAVDEHGSGSGGTRNISGTNHDHVLLEQELADLHGKEAGLLFTSGYVSNEATLSVVQKILPGLIIFSDELNHASMIAGIRNGGGPRKIFKHNDLAHLEQLLAEAPADAPKLIAFESVYSMDGDIADLAGTVALAKKYGAMTYLDEVHAVGMYGPRGGGVAERDGLMGEIDIIEGTLGKAFGVMGGYITGDAEVIDAIRLMASGFIFTTSLPPALTAGALASVRWLKQHPEVREIHQERAATLKAMFKAAGLPVMDSVSHIVPVLVGDPVHCKMISDMLLADFGVYVQPINYPTVPRGTERLRFTPTPFHTDDMMRKLVAAMEKLWAHCNVARMGGYAA
>biolip__7u7hA Cysteate acyl-acp transferase from alistipes finegoldii
MVDIFARLEKNAGGPIGQYMSYAHGYFAFPKLEGEIGPHMVFRGKKMLNWSLNNYLGLANHPEVRKADAEGAAKFGMAAPMGARMMSGQTVYHEQLERELAEFVGKEDAFLLNFGYQGMISIIDCLLTPRDVVVYDAEAHACIIDGLRLHKGKRFVYGHNDMDSLRLQLQHATDLAEEQKGGVLVITEGVFGMKGDLGKLDEIVALKKDFQFRLLVDDAHGFGTMGEGGRGTASHFGVTDGVDVLFNTFAKSMAGIGAFVCGPRWLVNLLRYNMRSQLYAKSLPMPMVMGALKRLELIRNHPEYQQKLWEIVRALQNGLKENGFEIGVTNSPVTPVFMKGGIPEATNLIVDLRENHGIFCSIVIYPVIPKGEIILRVIPTAAHTLDDVNYTIAAFKSVRDKLEGGIYAQMPIPVRADEGFKVR
>SwissProt__Q93UV0 Serine palmitoyltransferase; SPT; EC 2.3.1.50 (Sphingomonas paucimobilis (Pseudomonas paucimobilis))
MTEAAAQPHALPADAPDIAPERDLLSKFDGLIAERQKLLDSGVTDPFAIVMEQVKSPTEAVIRGKDTILLGTYNYMGMTFDPDVIAAGKEALEKFGSGTNGSRMLNGTFHDHMEVEQALRDFYGTTGAIVFSTGYMANLGIISTLAGKGEYVILDADSHASIYDGCQQGNAEIVRFRHNSVEDLDKRLGRLPKEPAKLVVLEGVYSMLGDIAPLKEMVAVAKKHGAMVLVDEAHSMGFFGPNGRGVYEAQGLEGQIDFVVGTFSKSVGTVGGFVVSNHPKFEAVRLACRPYIFTASLPPSVVATATTSIRKLMTAHEKRERLWSNARALHGGLKAMGFRLGTETCDSAIVAVMLEDQEQAAMMWQALLDGGLYVNMARPPATPAGTFLLRCSICAEHTPAQIQTVLGMFQAAGRAVGVIG
>PDB_5qrd_B Pandda analysis group deposition -- crystal structure of human alas2a in complex with z1328968520
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGV
GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV
FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK
IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLL
MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT
AVGLPLQCRRPVHFELMSEWERSYFGNM
>PDB_5qrb_B Pandda analysis group deposition -- crystal structure of human alas2a in complex with z2856434868
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGV
GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV
FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK
IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLL
MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT
AVGLPLQCRRPVHFELMSEWERSYFGNM
>PDB_5qr8_B Pandda analysis group deposition -- crystal structure of human alas2a in complex with z57258487
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGV
GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV
FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK
IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLL
MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT
AVGLPLQCRRPVHFELMSEWERSYFGNM
>PDB_5qr7_B Pandda analysis group deposition -- crystal structure of human alas2a in complex with z57299529
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGV
GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV
FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK
IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLL
MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT
AVGLPLQCRRPVHFELMSEWERSYFGNM
>PDB_5qr5_B Pandda analysis group deposition -- crystal structure of human alas2a in complex with z2241115980
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGV
GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV
FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK
IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLL
MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT
AVGLPLQCRRPVHFELMSEWERSYFGNM
>PDB_5qr4_B Pandda analysis group deposition -- crystal structure of human alas2a in complex with z2856434826
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGV
GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV
FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK
IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLL
MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT
AVGLPLQCRRPVHFELMSEWERSYFGNM
>PDB_5qqz_B Pandda analysis group deposition -- crystal structure of human alas2a in complex with z1675346324
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGV
GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV
FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK
IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLL
MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT
AVGLPLQCRRPVHFELMSEWERSYFGNM
>PDB_2xbn_A Inhibition of the plp-dependent enzyme serine palmitoyltransferase by cycloserine: evidence for a novel decarboxylative mechanism of inactivation
RDLLSKFDGLIAERQKLLDSGVTDPFAIVMEQVKSPTEAVIRGKDTILLGTYNYMGMTFDPDVIAAGKEALEKFGSGTNG
SRMLNGTFHDHMEVEQALRDFYGTTGAIVFSTGYMANLGIISTLAGKGEYVILDADSHASIYDGCQQGNAEIVRFRHNSV
EDLDKRLGRLPKEPAKLVVLEGVYSMLGDIAPLKEMVAVAKKHGAMVLVDEAHSMGFFGPNGRGVYEAQGLEGQIDFVVG
TFSKSVGTVGGFVVSNHPKFEAVRLACRPYIFTASLPPSVVATATTSIRKLMTAHEKRERLWSNARALHGGLKAMGFRLG
TETCDSAIVAVMLEDQEQAAMMWQALLDGGLYVNMARPPATPAGTFLLRCSICAEHTPAQIQTVLGMFQAAGRAVGVI
>PDB_2w8j_A Spt with plp-ser
RDLLSKFDGLIAERQKLLDSGVTDPFAIVMEQVKSPTEAVIRGKDTILLGTYNYMGMTFDPDVIAAGKEALEKFGSGTNG
SRMLNGTFHDHMEVEQALRDFYGTTGAIVFSTGYMANLGIISTLAGKGEYVILDADSHASIYDGCQQGNAEIVRFRHNSV
EDLDKRLGRLPKEPAKLVVLEGVYSMLGDIAPLKEMVAVAKKHGAMVLVDEAHSMGFFGPNGRGVYEAQGLEGQIDFVVG
TFSKSVGTVGGFVVSNHPKFEAVRLACRPYIFTASLPPSVVATATTSIRKLMTAHEKRERLWSNARALHGGLKAMGFRLG
TETCDSAIVAVMLEDQEQAAMMWQALLDGGLYVNMARPPATPAGTFLLRCSICAEHTPAQIQTVLGMFQAAGRAVGVI
>PDB_5qqr_B Pandda analysis group deposition -- crystal structure of human alas2a in complex with z1171217421
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGV
GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV
FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK
IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLL
MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT
AVGLPLQFCRRPVHFELMSEWERSYFGNM
>metacyc__HS08311-MONOMER 5-aminolevulinate synthase, erythroid-specific, mitochondrial (EC 2.3.1.37) (Homo sapiens)
MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGGDSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQEQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
>biolip__6hrhA Structure of human erythroid-specific 5'-aminolevulinate synthase, alas2
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTAVGLPLQNFCRRPVHFELMSEWERSYFGNM
>biolip__4bmkA Serine palmitoyltransferase k265a from s. Paucimobilis with bound plp- myriocin aldimine
RDLLSKFDGLIAERQKLLDSGVTDPFAIVMEQVKSPTEAVIRGKDTILLGTYNYMGMTFDPDVIAAGKEALEKFGSGTNGSRMLNGTFHDHMEVEQALRDFYGTTGAIVFSTGYMANLGIISTLAGKGEYVILDADSHASIYDGCQQGNAEIVRFRHNSVEDLDKRLGRLPKEPAKLVVLEGVYSMLGDIAPLKEMVAVAKKHGAMVLVDEAHSMGFFGPNGRGVYEAQGLEGQIDFVVGTFSASVGTVGGFVVSNHPKFEAVRLACRPYIFTASLPPSVVATATTSIRKLMTAHEKRERLWSNARALHGGLKAMGFRLGTETCDSAIVAVMLEDQEQAAMMWQALLDGGLYVNMARPPATPAGTFLLRCSICAEHTPAQIQTVLGMFQAAGRAVGVI
>PDB_5qre_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z117233350
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qrc_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z31721798
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qra_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z1101755952
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qr9_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z31478129
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qr3_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z915492990
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qr1_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z396380540
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qr0_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z730649594
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qqy_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z2856434899
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qqx_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z373768900
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qqw_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z136583524
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qqu_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z1348371854
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qqt_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z2856434834
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qqs_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z275151340
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>PDB_5qqq_A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z2856434857
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG
AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF
RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI
DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM
DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
>SwissProt__Q63147 5-aminolevulinate synthase, erythroid-specific, mitochondrial; ALAS-E; 5-aminolevulinic acid synthase 2; Delta-ALA synthase 2; Delta-aminolevulinate synthase 2; EC 2.3.1.37 (Rattus norvegicus (Rat))
MVAAAMLLRSCPVLSKGPTGLLGKVAKTYQFLFGIGRCPILATQGPTCSQIHLKATKAGADSPSWTKSHCPFMLSELQDRKSKIVQRAAPEVQEDVKTFKTDLLSFMESTTRSQSVPRFQDPEQTGGAPPLLIQNNMTGSQAFGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAQHFSEASMDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKLDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVGNAALNSKICDLLLAKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTEVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
>BRENDA__A0QX65 8-amino-7-oxononanoate synthase (EC 2.3.1.47) (Mycolicibacterium smegmatis)
MTRAGLSPLAWLADIEQRRRAEGLRRELRVRPPVAAELDLASNDYLGLSQHPDVLDGGVEALRTWGGGAGGSRLVTGNTELHEAFEHQLASFLGAESALVFSSGYTANLGALVALSGPGSLIVSDALSHASLVDACRLSRARVVVSPHRDVDAVDAALAARTEERAVVVTESVFSADGDLAPLRDLHAVCRRHGALLLVDEAHGLGVRGTRGQGLLHEVGLAGAPDIVMTTTLSKALGSQGGAVLGPEAVRAHLIDTARSFIFDTGLAPAAVGAASAALRVLDAEPQRARAVLDRAAELATIAGVTEAPVSAVVSVILGDPEIAVGAAAACLDRGVRVGCFRPPTVPAGTSRLRLAARASLTDDEMALARQVLTDVLATARA
>SwissProt__P08680 5-aminolevulinate synthase, erythroid-specific, mitochondrial; ALAS-E; 5-aminolevulinic acid synthase 2; Delta-ALA synthase 2; Delta-aminolevulinate synthase 2; EC 2.3.1.37 (Mus musculus (Mouse))
MVAAAMLLRSCPVLSQGPTGLLGKVAKTYQFLFSIGRCPILATQGPTCSQIHLKATKAGGDSPSWAKSHCPFMLSELQDRKSKIVQRAAPEVQEDVKTFKTDLLSTMDSTTRSHSFPSFQEPEQTEGAVPHLIQNNMTGSQAFGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAQHFSEASMASKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGARGAGIGERDGIMHKLDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVGNAALNSKICDLLLSKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTEVGLPLQDVSVAACNFCHRPVHFELMSEWERSYFGNMGPQYVTTYA
>SwissProt__O14092 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinic acid synthase; Delta-ALA synthase; Delta-aminolevulinate synthase; EC 2.3.1.37 (Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast))
MERVVKLAAKHCPFVSKADPSALRRMAGAGLIRAGARCPVVRHALPVAAATGADVSRGFKSDSKQMAMEPSLDEIHLKAGVVNTGSRTCRHADAVKAAAEAATTTPVTKKHQMPKHYASDLNGVGPATTPRFDYDTFYREELDKKHRDKSYRYFNNINRLAKEYPLAHLADPNTRVEVWCSNDYLNMGGHKKIREAMHQCIETYGGGAGGTRNIAGHNQHAVRLEKSLADLHQKPAALVFGSCYVANDATLSTLGRKLPNCIFLSDEMNHASMINGIRNSRCEKIIFKHNDLVDLEAKLASLPLNRPKIIAFESVYSMSGNVAPISEICDLAKKYGAITFLDEVHAVGMYGPRGAGVAEETPGLLSRVDIITGTLAKSYGCVGGYIAASSTLVDMIRSLAPGFIFTTSLPPHVMVGALTAVEHLKVSNVEREQQRSAVRRVKQSLSEIGIPVLSNDTHIVPAMVGDAHLAKLASDSLLHDHNIYVQSINFPTVSVGTERLRITPTPAHNTEHYVQSLTNAMNDVWSKFNINRIDGWEKRGIDVGRLCKFPVLPFTTTH
>metacyc__MONOMER-18786 bifunctional 5-aminolevulinate synthase / 5-aminolevulinyl-CoA cyclase (EC 2.3.1.37) (Streptomyces aizunensis)
MNLHLESYSTGVTAKELAERRREFLEIGRRSGHFPSASARQDGVDSQISVWCSNDYLGMGQNPQVIEAMKKTIDTHGVGSGGSRNIGGTNHYHVLLEAELADLHGKEAALLFTSGYTANDGSLSVLAGTPKDTIVFSDEKNHASIIDGLRHSGAQKHIFRHNDVAHLAELLAAAPADRPKLIVLESVYSMSGDIAPLAEIAELARRYDATTYIDEVHAVGMYGPQGAGIAAREGIADQFTVVMGTLAKGYGTVGGYIAGPAALVDAVRTLSRAFVFTTSLPPAVAAGALEAVRYLRNSDVERKVLAENAQLLHRLLDEADIPFISPDSHIVSAFIGDDETCKQASRLLFERHGIYVQSINAPSVPLGQEILRIAPSTVHGREDVENFAEALRGIWKELNIPTATDRNWLS
>BRENDA__Q68F30 5-aminolevulinate synthase (EC 2.3.1.37) (Xenopus laevis)
MASLINRCPFATRDPTVFLRVARPFLLRSAERCPIMVTRSLSTSAGCEQRAKDIPPATGVSTGASNRRTLAQAAPQAAIANATCPFIENEIGKGEGSIVQRAGPQVQEDISAFKTDALSSLLIEVQSSLKKKFLTPSSKKVNLGTGAPLIPTHLIKENISGRAAFGYDDFFSRRIEEKKSDHTYRVFKTVNRRADAYPFAEDYSDLHGEKKEVSVWCSNDYLGMSRHPRVLKAISEALQEHGAGAGGTRNISGTSKYHVDLECELADLHNKDAALLFSSCFVANDSALFTLAKMLPGCEIYSDAGNHASMIQGIRNSGVTKFVFRHNDPAHLEELLQKADPKTPKIVAFETVHSMDGAICPLEEMCDVAHKYGAMTFVDEVHAVGLYGTHGAGVGERDGVMHKMDIISGTLGKAFGCVGGYIASTASLIDTVRSYAAGFIFTTSLPPMVLAGAVESVRVLKSEEGQALRRAHQRNVKHMRQLLMDAGLPVINCPSHIIPIRVGNAAINSRICDVLLSQYNIYVQAINYPTVPRGEELLRLAPSPHHTPDMMTYFVESVVSAWKEVGMPLHTPSAAECNFCHRPLHFDLMSEWERTYFGNMEPKYITMYA
>biolip__5txrA Structure of alas from s. Cerevisiae non-covalently bound to plp cofactor
GFDYEGLIDSELQKKRLDKSYRYFNNINRLAKEFPLAHRQREADKVTVWCSNDYLALSKHPEVLDAMHKTIDKYGCGAGGTRNIAGHNIPTLNLEAELATLHKKEGALVFSSCYVANDAVLSLLGQKMKDLVIFSDELNHASMIVGIKHANVKKHIFKHNDLNELEQLLQSYPKSVPKLIAFESVYSMAGSVADIEKICDLADKYGALTFLDEVHAVGLYGPHGAGVAEHCDFESHRASGIATPKTNDKGGAKTVMDRVDMITGTLGKSFGSVGGYVAASRKLIDWFRSFAPGFIFTTTLPPSVMAGATAAIRYQRCHIDLRTSQQKHTMYVKKAFHELGIPVIPNPSHIVPVLIGNADLAKQASDILINKHQIYVQAINFPTVARGTERLRITPTPGHTNDLSDILINAVDDVFNELQLPRVRDWESQGGLLGVGESGFVEESNLWTSSQLSLTNDDLNPNVRDPIVKQLEVSSGIKQ
>SwissProt__P09950 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinic acid synthase; Delta-ALA synthase; Delta-aminolevulinate synthase; EC 2.3.1.37 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast))
MQRSIFARFGNSSAAVSTLNRLSTTAAPHAKNGYATATGAGAAAATATASSTHAAAAAAAAANHSTQESGFDYEGLIDSELQKKRLDKSYRYFNNINRLAKEFPLAHRQREADKVTVWCSNDYLALSKHPEVLDAMHKTIDKYGCGAGGTRNIAGHNIPTLNLEAELATLHKKEGALVFSSCYVANDAVLSLLGQKMKDLVIFSDELNHASMIVGIKHANVKKHIFKHNDLNELEQLLQSYPKSVPKLIAFESVYSMAGSVADIEKICDLADKYGALTFLDEVHAVGLYGPHGAGVAEHCDFESHRASGIATPKTNDKGGAKTVMDRVDMITGTLGKSFGSVGGYVAASRKLIDWFRSFAPGFIFTTTLPPSVMAGATAAIRYQRCHIDLRTSQQKHTMYVKKAFHELGIPVIPNPSHIVPVLIGNADLAKQASDILINKHQIYVQAINFPTVARGTERLRITPTPGHTNDLSDILINAVDDVFNELQLPRVRDWESQGGLLGVGESGFVEESNLWTSSQLSLTNDDLNPNVRDPIVKQLEVSSGIKQ
>SwissProt__P13195 5-aminolevulinate synthase, non-specific, mitochondrial; ALAS-H; 5-aminolevulinic acid synthase 1; Delta-ALA synthase 1; Delta-aminolevulinate synthase 1; EC 2.3.1.37 (Rattus norvegicus (Rat))
METVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRTVSTSAAQCQQVKETPPANEKEKTAKAAVQQAPDESQMAQTPDGTQLPPGHPSPSTSQSSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMHAVRKEVAQSPVLPSLVNAKRDGEGPSPLLKNFQDIMRKQRPERVSHLLQDNLPKSVSTFQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSLITKKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSNEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKRVGLELKPHSSAECNFCRRPLHFEVMSEREKAYFSGMSKMVSAQA
>metacyc__MONOMER-13234 5-aminolevulinate synthase 2 (EC 2.3.1.37) (Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.))
MEFSQHFQKLIDDMRLDGRYRTFAELERIAGEFPTALWHGPDGQARRVTVWCSNDYLGMGQNAEVLAAMHRSIDLSGAGTGGTRNISGTNRQHVALEAELADLHGKESALIFTSGWISNLAALGTLGKILPECAIFSDALNHNSMIEGIRRSGAERFIFHHNDPVHLDRLLSSVDPARPKIVAFESVYSMDGDIAPIAEICDVAERHGALTYLDEVHAVGLYGPRGGGISDRDGLADRVTIIEGTLAKAFGVMGGYVSGPSLLMDVIRSMSDSFIFTTSICPHLAAGALAAVRHVKAHPDERRRQAENAVRLKVLLQKAGLPVLDTPSHILPVMVGEAHLCRSISEALLARHAIYVQPINYPTVARGQERFRLTPTPFHTTSHMEALVEALLAVGRDLGWAMSRRAA
>BRENDA__Q04512 5-aminolevulinate synthase (EC 2.3.1.37) (Cereibacter sphaeroides)
MDYNLALDTALNRLHTEGRYRTFIDIERRKGAFPKAMWRKPDGSEKEITVWCGNDYLGMGQHPVVLGAMHEALDSTGAGSGGTRNISGTTLYHKRLEAELADLHGKEAALVFSSAYIANDATLSTLPQLIPGLVIVSDKLNHASMIEGIRRSGTEKHIFKHNDLDDLRRILTSIGKDRPILVAFESVYSMDGDFGRIEEICDIADEFGALKYIDEVHAVGMYGPRGGGVAERDGLMDRIDIINGTLGKAYGVFGGYIAASSKMCDAVRSYAPGFIFSTSLPPVVAAGAAASVRHLKGDVELREKHQTQARILKMRLKGLGLPIIDHGSHIVPVHVGDPVHCKMISDMLLEHFGIYVQPINFPTVPRGTERLRFTPSPVHDSGMIDHLVKAMDVLWQHCALNRAEVVA
>SwissProt__Q09925 Serine palmitoyltransferase 2; SPT 2; Long chain base biosynthesis protein 2; EC 2.3.1.50 (Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast))
MAQADFVSPTSIDVSEKKEVEFHKKVDHVENPPLSTESAKLEAEEVAAEKLNSEHLLENEFAPITDPTHRRVSKNPDGAELFQFEDEPSYYYVVATYLTYLVLIIIGHVRDFFGKRFHKDDYKYLKDNDGYAPLYNHFDNFYVRRLQHRINDCFSRPTMGVPGRVIRLMNRYSTDSNSTFKLTGDTSLALNVSSYNYLGFAQSHGPCATKVEEAMQKYGLSTCSSNAICGTYGLHKEVEELTANFVGKPAALVFSQGFSTNATVFSTLMCPGSLIISDELNHTSIRFGARLSGANIRVYKHNDMTDLERVLREVISQGQPRTHRPYSKILVVIEGLYSMEGNFCDLPKVVELKNRYKFYLFIDEAHSIGAIGPRGGGICDYFGISTDHVDILMGTFTKSFGAAGGYISATPNIINKLRVTNPGYVYAESMSPAVLAQIKSSFLEIMDNSPTSAGLERIERLAFNSRYIRLGLKRLGFIIFGNDDSPVVPLLLYNPGKINAFSHEMLKRGIAVVVVGYPACPLLTSRVRFCFSASHNKADMDYFLRACDEVGEKLQLKFSTGAAGEDVGKTNVEKMKKNQGWFKPPRWKIEDVLKHGVHDALTQ
>CharProtDB__CH_123079 5-aminolevulinate synthase, mitochondrial; EC 2.3.1.37 (Candida albicans)
MESITKVSMSVCPFVRSTSTQALRQLSQTSGALANQARQCPIAGNAIRAKEISIRSYSSATKPVRATAATPSTPEATFNVSSSFELGSKETAFDYNGYLGNELEKKRSDKSYRYFNNINRLANEFPKAHRTQEEDKVTVWCSNDYLGMGKNENTLKEMKRVLDKYGSGAGGTRNIAGHNSHAIKLESELAALHKHDAALVFSSCFVANDAVLSLLGQKIKDLVIFSDELNHASMIQGIRNSRARKHIFKHNNLADLESKLAQYPKSTPKLIAFESVYSMCGSIAPIEAICDLAEKYGALTFLDEVHAVGMYGPHGAGVAEHLNFEAHLKSGIERPEITTVMSRVDMVTGTLGKAYGVVGGYITGKTNLIDWFRSYAPGFIFTTSLPPAIMAGCSASIRYQRATLKDRIAQQKNTRLVKNNLNELGIPVIPNPSHIVPVLVGNAADAKRASDLLLNKHDIYVQAINFPTVPIGEERLRITPTPGHGPELSKQLVEAVDSVFTELNLNRINDWKKLGGLVGVGVEGAAKVEHIWTEEQLALTDADLNPNVVNPAISPLDVSSGIST
>SwissProt__P18079 5-aminolevulinate synthase; 5-aminolevulinic acid synthase; Delta-ALA synthase; Delta-aminolevulinate synthase; EC 2.3.1.37 (Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003))
MDYNLALDKAIQKLHDEGRYRTFIDIEREKGAFPKAQWNRPDGGKQDITVWCGNDYLGMGQHPVVLAAMHEALEAVGAGSGGTRNISGTTAYHRRLEAEIADLHGKEAALVFSSAYIANDATLSTLRVLFPGLIIYSDSLNHASMIEGIKRNAGPKRIFRHNDVAHLRELIAADDPAAPKLIAFESVYSMDGDFGPIKEICDIADEFGALTYIDEVHAVGMYGPRGAGVAERDGLMHRIDIFNGTLAKAYGVFGGYIAASAKMVDAVRSYAPGFIFSTSLPPAIAAGAQASIAFLKTAEGQKLRDAQQMHAKVLKMRLKALGMPIIDHGSHIVPVVIGDPVHTKAVSDMLLSDYGVYVQPINFPTVPRGTERLRFTPSPVHDLKQIDGLVHAMDLLWARCALNRAEASA
>metacyc__HS16070-MONOMER SPTLC3 (Homo sapiens)
MANPGGGAVCNGKLHNHKKQSNGSQSRNCTKNGIVKEAQQNGKPHFYDKLIVESFEEAPLHVMVFTYMGYGIGTLFGYLRDFLRNWGIEKCNAAVERKEQKDFVPLYQDFENFYTRNLYMRIRDNWNRPICSAPGPLFDLMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAAKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTRRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDGTTQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKKSARPELYDETSFELED
>SwissProt__P9WQ87 8-amino-7-oxononanoate synthase 1; AONS; 7-keto-8-amino-pelargonic acid synthase; 7-KAP synthase; KAPA synthase; 8-amino-7-ketopelargonate synthase; EC 2.3.1.47 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
MKAATQARIDDSPLAWLDAVQRQRHEAGLRRCLRPRPAVATELDLASNDYLGLSRHPAVIDGGVQALRIWGAGATGSRLVTGDTKLHQQFEAELAEFVGAAAGLLFSSGYTANLGAVVGLSGPGSLLVSDARSHASLVDACRLSRARVVVTPHRDVDAVDAALRSRDEQRAVVVTDSVFSADGSLAPVRELLEVCRRHGALLLVDEAHGLGVRGGGRGLLYELGLAGAPDVVMTTTLSKALGSQGGVVLGPTPVRAHLIDAARPFIFDTGLAPAAVGAARAALRVLQAEPWRPQAVLNHAGELARMCGVAAVPDSAMVSVILGEPESAVAAAAACLDAGVKVGCFRPPTVPAGTSRLRLTARASLNAGELELARRVLTDVLAVARR