>WP_007474399.1 NCBI__GCF_000170735.1:WP_007474399.1
MQGAMTALITPFRNGKVDEETYAKLIQRQIDNDIDWVVPVGTTGESATLTHDEHKKCIEIAVEVCKGTDTKVLAGAGSNSTHEAIDLAKFAQQKGADAILSVAPYYNKPTQKGLYEHYKALAESIEIPLVLYNVPGRTCSNIEVETAIRLFNDVENIVAIKEATGKIENVVALCSKCAISVISGDDAINYPIIATGGKGVISVASNLVPKKIAKLVHKALKGDFIKAREINEELYDLNKVLFIESNPIPIKYAMYEAGLIPSLEYRLPLVEPSEESKRKIKEVIKRYL
>PDB_4m19_A Dihydrodipicolinate synthase from c. Jejuni with pyruvate bound to the active site and lysine bound to allosteric site
KNIIIGAMTALITPFKNGKVDEQSYARLIKRQIENGIDAVVPVGTTGESATLTHEEHRTCIEIAVETCKGTKVKVLAGAG
SNATHEAVGLAKFAKEHGADGILSVAPYYNKPTQQGLYEHYKAIAQSVDIPVLLYNVPGRTGCEISTDTIIKLFRDCENI
YGVKEASGNIDKCVDLLAHEPRMMLISGEDAINYPILSNGGKGVISVTSNLLPDMISALTHFALDENYKEAKKINDELYN
INKILFCESNPIPIKTAMYLAGLIESLEFRLPLCSPSKENFAKIEEVMKKYKIKGF
>PDB_6u01_B Dihydrodipicolinate synthase (dhdps) from c.Jejuni, n84d mutant with pyruvate bound in the active site
KNIIIGAMTALITPFKNGKVDEQSYARLIKRQIENGIDAVVPVGTTGESATLTHEEHRTCIEIAVETCKGTKVKVLAGAG
SDATHEAVGLAKFAKEHGADGILSVAPYYNKPTQQGLYEHYKAIAQSVDIPVLLYNVPGRTGCEISTDTIIKLFRDCENI
YGVKEASGNIDKCVDLLAHEPRMMLISGEDAINYPILSNGGKGVISVTSNLLPDMISALTHFALDENYKEAKKINDELYN
INKILFCESNPIPIKTAMYLAGLIESLEFRLPLCSPSKENFAKIEEVMKKYKIKGF
>biolip__7kkdB Dihydrodipicolinate synthase (dhdps) from c.Jejuni, n84a mutant with pyruvate bound in the active site and r,r-bislysine bound at the allosteric site
HHHHHHGSMDKNIIIGAMTALITPFKNGKVDEQSYARLIKRQIENGIDAVVPVGTTGESATLTHEEHRTCIEIAVETCKGTKVKVLAGAGSAATHEAVGLAKFAKEHGADGILSVAPYYNKPTQQGLYEHYKAIAQSVDIPVLLYNVPGRTGCEISTDTIIKLFRDCENIYGVKEASGNIDKCVDLLAHEPRMMLISGEDAINYPILSNGGKGVISVTSNLLPDMISALTHFALDENYKEAKKINDELYNINKILFCESNPIPIKTAMYLAGLIESLEFRLPLCSPSKENFAKIEEVMKKYKIKGF
>PDB_7kg2_A Dihydrodipicolinate synthase (dhdps) from c.Jejuni, h59k mutant with pyruvate bound in the active site and l-histidine bound at the allosteric site
KNIIIGAMTALITPFKNGKVDEQSYARLIKRQIENGIDAVVPVGTTGESATLTHEEKRTCIEIAVETCKGTKVKVLAGAG
SNATHEAVGLAKFAKEHGADGILSVAPYYNKPTQQGLYEHYKAIAQSVDIPVLLYNVPGRTGCEISTDTIIKLFRDCENI
YGVKEASGNIDKCVDLLAHEPRMMLISGEDAINYPILSNGGKGVISVTSNLLPDMISALTHFALDENYKEAKKINDELYN
INKILFCESNPIPIKTAMYLAGLIESLEFRLPLCSPSKENFAKIEEVMKKYKIKGF
>BRENDA__O67216 4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7) (Aquifex aeolicus)
MFQGSIVALITPFKEGEVDYEALGNLIEFHVDNGTDAILVCGTTGESPTLTFEEHEKVIEFAVKRAAGRIKVIAGTGGNATHEAVHLTAHAKEVGADGALVVVPYYNKPTQRGLYEHFKTVAQEVDIPIIIYNIPSRTCVEISVDTMFKLASECENIVASKESTPNMDRISEIVKRLGESFSVLSGDDSLTLPMMALGAKGVISVANNVMPREVKELIRAALEGDFRRAREIHYYLHDLFKVLFIETNPIPVKTACWMLGMCEKEFRLPLTEMSPENENKLREVLKKYNLPLKN
>SwissProt__Q57695 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 (Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii))
MFKGVYPAIITPFKNKEVDFDGLEENINFLIENGVSGIVAVGTTGESPTLSHEEHKKVIEKVVDVVNGRVQVIAGAGSNCTEEAIELSVFAEDVGADAVLSITPYYNKPTQEGLRKHFGKVAESINLPIVLYNVPSRTAVNLEPKTVKLLAEEYSNISAVKEANPNLSQVSELIHDAKITVLSGNDELTLPIIALGGKGVISVVANIVPKEFVEMVNYALEGDFEKAREIHYKLFPLMKAMFIETNPIPVKTALNMMGRPAGELRLPLCEMSEEHKKILENVLKDLGLI
>BRENDA__A5F699 4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7) (Vibrio cholerae)
MFSGSIVALITPFTPDGEVDYISLKKLVDFHVDAGTDAIVSVGTTGESATLTVEEHVKVVAKTVEFAEGRLPIIAGTGANATHEAVTFSRLLNNTGIAGYLSVTPYYNKPTQEGLFLHYNAIAQETDIPVILYNVPGRTAVDMRPETVARLSEIKNIVALKDATGDLSRVAKHREMCKEGFVLLSGDDATGLEFVKLGGQGVISVTNNIAAADMAKMMHLALDGKFDEAASINQRLMTLHKNLFIESSPIPVKWAAHKMGLIANGDLRLPLTQLSEPARPIVAQALSEACIY
>SwissProt__Q9X1K9 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
MFRGVGTAIVTPFKNGELDLESYERLVRYQLENGVNALIVLGTTGESPTVNEDEREKLVSRTLEIVDGKIPVIVGAGTNSTEKTLKLVKQAEKLGANGVLVVTPYYNKPTQEGLYQHYKYISERTDLGIVVYNVPGRTGVNVLPETAARIAADLKNVVGIKEANPDIDQIDRTVSLTKQARSDFMVWSGNDDRTFYLLCAGGDGVISVVSNVAPKQMVELCAEYFSGNLEKSREVHRKLRPLMKALFVETNPIPVKAALNLMGFIENELRLPLVPASEKTVELLRNVLKESGLL
>biolip__1o5kA Crystal structure of dihydrodipicolinate synthase (tm1521) from thermotoga maritima at 1.80 a resolution
HMFRGVGTAIVTPFKNGELDLESYERLVRYQLENGVNALIVLGTTGESPTVNEDEREKLVSRTLEIVDGKIPVIVGAGTNSTEKTLKLVKQAEKLGANGVLVVTPYYNKPTQEGLYQHYKYISERTDLGIVVYNVPGRTGVNVLPETAARIAADLKNVVGIKEANPDIDQIDRTVSLTKQARSDFMVWSGNDDRTFYLLCAGGDGVISVVSNVAPKQMVELCAEYFSGNLEKSREVHRKLRPLMKALFVETNPIPVKAALNLMGFIENELRLPLVPASEKTVELLRNVLKESGLL
>biolip__4dxvA Crystal structure of dihydrodipicolinate synthase from acinetobacter baumannii complexed with mg and cl ions at 1.80 a resolution
TIQGSIVAIVTPMLKDGGVDWKSLEKLVEWHIEQGTNSIVAVGTTGEASTLSMEEHTQVIKEIIRVANKRIPIIAGTGANSTREAIELTKAAKDLGADAALLVTPYYNKPTQEGLYQHYKAIAEAVELPLILYNVPGRTGVDLSNDTAVRLAEIPNIVGIKDATGDVPRGKALIDALNGKMAVYSGDDETAWELMLLGADGNISVTANIAPKAMSEVCAVAIAKDEQQAKTLNNKIANLHNILFCESNPIPVKWALHEMGLIDTGIRLPLTPLAEQYREPLRNALKDAGII
>PDB_3u8g_A Crystal structure of the complex of dihydrodipicolinate synthase from acinetobacter baumannii with oxalic acid at 1.80 a resolution
TIQGSIVAIVTPMLKDGGVDWKSLEKLVEWHIEQGTNSIVAVGTTGEASTLSMEEHTQVIKEIIRVANKRIPIIAGTGAN
STREAIELTKAAKDLGADAALLVTPYYNKPTQEGLYQHYKAIAEAVELPLILYNVPGRTGVDLSNDTAVRLAEIPNIVGI
KDATGDVPRGKALIDALNGKMAVYSGDDETAWELMLLGADGNISVTANIAPKAMSEVCAVAIAKDEQQAKTLNNKIANLH
NILFCESNPIPVKWALHEMGLIDTGIRLPLTPLAEQYREPLRNALKDAGII
>PDB_3tdf_A Crystal structure of the complex of dihydrodipicolinate synthase from acinetobacter baumannii with 2-ketobutanoic acid at 1.99 a resolution
TIQGSIVAIVTPMLKDGGVDWKSLEKLVEWHIEQGTNSIVAVGTTGEASTLSMEEHTQVIKEIIRVANKRIPIIAGTGAN
STREAIELTKAAKDLGADAALLVTPYYNKPTQEGLYQHYKAIAEAVELPLILYNVPGRTGVDLSNDTAVRLAEIPNIVGI
KDATGDVPRGKALIDALNGKMAVYSGDDETAWELMLLGADGNISVTANIAPKAMSEVCAVAIAKDEQQAKTLNNKIANLH
NILFCESNPIPVKWALHEMGLIDTGIRLPLTPLAEQYREPLRNALKDAGII
>PDB_3tce_A Crystal structure of the complex of dihydrodipicolinate synthase from acinetobacter baumannii with 5-hydroxylysine at 2.6 a resolution
TIQGSIVAIVTPMLKDGGVDWKSLEKLVEWHIEQGTNSIVAVGTTGEASTLSMEEHTQVIKEIIRVANKRIPIIAGTGAN
STREAIELTKAAKDLGADAALLVTPYYNKPTQEGLYQHYKAIAEAVELPLILYNVPGRTGVDLSNDTAVRLAEIPNIVGI
KDATGDVPRGKALIDALNGKMAVYSGDDETAWELMLLGADGNISVTANIAPKAMSEVCAVAIAKDEQQAKTLNNKIANLH
NILFCESNPIPVKWALHEMGLIDTGIRLPLTPLAEQYREPLRNALKDAGII
>PDB_3rk8_A Crystal structure of the chloride inhibited dihydrodipicolinate synthase from acinetobacter baumannii complexed with pyruvate at 1.8 a resolution
TIQGSIVAIVTPMLKDGGVDWKSLEKLVEWHIEQGTNSIVAVGTTGEASTLSMEEHTQVIKEIIRVANKRIPIIAGTGAN
STREAIELTKAAKDLGADAALLVTPYYNKPTQEGLYQHYKAIAEAVELPLILYNVPGRTGVDLSNDTAVRLAEIPNIVGI
KDATGDVPRGKALIDALNGKMAVYSGDDETAWELMLLGADGNISVTANIAPKAMSEVCAVAIAKDEQQAKTLNNKIANLH
NILFCESNPIPVKWALHEMGLIDTGIRLPLTPLAEQYREPLRNALKDAGII
>PDB_3pue_B Crystal structure of the complex of dhydrodipicolinate synthase from acinetobacter baumannii with lysine at 2.6a resolution
TIQGSIVAIVTPMLKDGGVDWKSLEKLVEWHIEQGTNSIVAVGTTGEASTLSMEEHTQVIKEIIRVANKRIPIIAGTGAN
STREAIELTKAAKDLGADAALLVTPYYNKPTQEGLYQHYKAIAEAVELPLILYNVPGRTGVDLSNDTAVRLAEIPNIVGI
KDATGDVPRGKALIDALNGKMAVYSGDDETAWELMLLGADGNISVTANIAPKAMSEVCAVAIAKDEQQAKTLNNKIANLH
NILFCESNPIPVKWALHEMGLIDTGIRLPLTPLAEQYREPLRNALKDAGII
>SwissProt__Q9I4W3 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 (Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1))
MIAGSMVALVTPFDAQGRLDWDSLAKLVDFHLQEGTNAIVAVGTTGESATLDVEEHIQVIRRVVDQVKGRIPVIAGTGANSTREAVALTEAAKSGGADACLLVTPYYNKPTQEGMYQHFRHIAEAVAIPQILYNVPGRTSCDMLPETVERLSKVPNIIGIKEATGDLQRAKEVIERVGKDFLVYSGDDATAVELMLLGGKGNISVTANVAPRAMSDLCAAAMRGDAAAARAINDRLMPLHKALFIESNPIPVKWALHEMGLIPEGIRLPLTWLSPRCHEPLRQAMRQTGVLA
>SwissProt__Q07607 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; Protein MosA; EC 4.3.3.7 (Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti))
MFEGSITALVTPFADDRIDEVALHDLVEWQIEEGSFGLVPCGTTGESPTLSKSEHEQVVEITIKTANGRVPVIAGAGSNSTAEAIAFVRHAQNAGADGVLIVSPYYNKPTQEGIYQHFKAIDAASTIPIIVYNIPGRSAIEIHVETLARIFEDCPNVKGVKDATGNLLRPSLERMACGEDFNLLTGEDGTALGYMAHGGHGCISVTANVAPALCADFQQACLNGDFAAALKLQDRLMPLHRALFLETNPAGAKYALQRLGRMRGDLRLPLVTISPSFQEEIDDAMRHAGILL
>BRENDA__Q8RBI5 4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7) (Caldanaerobacter subterraneus subsp. tengcongensis)
MPVFKGSCVAIVTPFTENGVNFDKLGELIEWHIKEGTDAILICGTTGEASTMTDEEQKEAIKFTVEKVAKRIPVIAGTGSNNTAHAIELSEYAQSVGADALLVITPYYNKTTQKGLVAHFTEIARHVDIPIIIYNVPSRTSLNMLPETYLEVKKKAENVVGVKEASGDISQIAEIARIMGKSFEIYSGNDDQVIPIMSLGGLGVISVTANIIPAKIHEMTTAYLNGDIEKARDMQLELNPLNKALFIETNPIPVKTAMNLMGFGVGPLRLPLVEMSEKNLEYLKSVLRQYGLLKEEN
>BRENDA__Q6G468 4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7) (Bartonella henselae)
MLKGAVTALITPFDDNGAIDEKAFCNFVEWQITQGINGVSPVGTTGESPTLTHEEHKRIIELCVEQVAKRVPVVAGAGSNSTSEAVELAKHAEKAGADAVLVVTPYYNRPNQRGLYTHFSSIAKAISIPIIIYNIPSRSVIDMAVETMRDLCRDFKNIIGVKDATGKIERASEQREKCGKDFVQLSGDDCTALGFNAHGGVGCISVSSNVAPKLCAQLHAACLCSDYKTALKLNDLLMPLNRAVFIEPSPAGIKYAAAKLGLCGTIVRSPIVPLSDTTKKIIDEALYHAGLLKE
>ENA__CAC50571.1 dihydrodipicolinate synthetase (Yersinia enterocolitica)
MFTGSIVALITPMDDKGNVDRASLKKLIDYHVASGTAAIVSVGTTGESATLNHDEHVDVVLQTLELADGRIPVIAGTGANATSEAISLTQRFNDTGVVGCLTVTPYYNRPMQEGLYQHFKAIAESTDLPQILYNVPSRTGCDMLPPTIARLAKIKNIVAVKEATGNLSRVSQIQVLVDDEDFILLSGDDASGLDFMQLGGQGVISVTANIAAREMVELCALAAQGNFAEARRLNQRLMPLHQHLFVEANPIPVKWAAKKLGLMANDTLRLPMTPLTDPAKRVVEDALKSAGLL
>biolip__3puoA Crystal structure of dihydrodipicolinate synthase from pseudomonas aeruginosa(psdhdps)complexed with l-lysine at 2.65a resolution
MIAGSMVALVTPFDAQGRLDWDSLAKLVDFHLQDGTNAIVAVGTTGESATLDVEEHIQVVRRVVDQVKGRIPVIAGTGANSTREAVALTEAAKSGGADACLLVTPYYNKPTQEGMYQHFRHIAEAVAIPQILYNVPGRTSCDMLPETVERLSKVPNIIGIKEATGDLQRAKEVIERVGKDFLVYSGDDATAVELMLLGGKGNISVTANVAPRAMSDLCAAAMRGDAAAARAINDRLMPLHKALFIESNPIPVKWALHEMGLIPEGIRLPLTWLSPHCHDPLRQAMRQTGVLA
>SwissProt__Q9JZR4 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 (Neisseria meningitidis serogroup B (strain MC58))
MLQGSLVALITPMNQDGSIHYEQLRDLIDWHIENGTDGIVAVGTTGESATLSVEEHTAVIEAVVKHVAKRVPVIAGTGANNTVEAIALSQAAEKAGADYTLSVVPYYNKPSQEGIYQHFKTIAEATSIPMIIYNVPGRTVVSMTNDTILRLAEIPNIVGVKEASGNIGSNIELINRAPEGFVVLSGDDHTALPFMLCGGHGVITVAANAAPKLFADMCRAALQGDIALARELNDRLIPIYDTMFCEPSPAAPKWAVSALGRCEPHVRLPLVPLTENGQAKVRAALKASGQL
>PDB_3s8h_A Structure of dihydrodipicolinate synthase complexed with 3- hydroxypropanoic acid(hpa)at 2.70 a resolution
MIAGSMVALVTPFDAQGRLDWDSLAKLVDFHLQDGTNAIVAVGTTGESATLDVEEHIQVVRRVVDQVKGRIPVIAGTGAN
STREAVALTEAAKSGGADACLLVTPYYNKPTQEGMYQHFRHIAEAVAIPQILYNVPGRTSCDMLPETVERLSKVPNIIGI
KEATGDLQRAKEVIERVGKDFLVYSGDDATAVELMLLGGKGNISVTANVAPRAMSDLCAAAMRGDAAAARAINDRLMPLH
KALFIESNPIPVKWALHEMGLIPEGIRLPLTWLSPHCHDPLRQAMRQTGVLA
>biolip__4i7wA Agrobacterium tumefaciens dhdps with lysine and pyruvate
MFKGSIPALITPFTDNGAVDEQAFAAHVEWQIAEGSNGLVPVGTTGESPTLSHDEHKRVVELCIEVAAKRVPVIAGAGSNNTDEAIELALHAQDAGADALLVVTPYYNKPTQKGLFAHFSAVAEAVKLPIVIYNIPPRSVVDMSPETMGALVKAHKNIVGVKDATGKLDRVSEQRISCGKDFIQLSGEDSTALGFNAHGGVGCISVSANVAPRLCSEFQAAMLAGDYAKALEYQDRLMPLHRAIFMEPGVCGTKYALSKTRGCNRKVRSPLMSTLEPATEAAIDAALKHAGLMN
>CharProtDB__CH_021853 dihydrodipicolinate synthase; EC 4.2.1.52 (Bacillus anthracis)
MIDFGTIATAMVTPFDINGNIDFAKTTKLVNYLIDNGTTAIVVGGTTGESPTLTSEEKVALYRHVVSVVDKRVPVIAGTGSNNTHASIDLTKKATEVGVDAVMLVAPYYNKPSQEGMYQHFKAIAESTPLPVMLYNVPGRSIVQISVDTVVRLSEIENIVAIKDAGGDVLTMTEIIEKTADDFAVYSGDDGLTLPAMAVGAKGIVSVASHVIGNEMQEMIAAFQAGEFKKAQKLHQLLVRVTDSLFMAPSPTPVKTALQMVGLDVGSVRLPLLPLTEEERVTLQSVMQSIPR
>SwissProt__Q8UGL3 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 (Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)))
MFKGSIPALITPFTDNGSVDEKAFAAHVEWQIAEGSNGLVPVGTTGESPTLSHDEHKRVVELCIEVAAKRVPVIAGAGSNNTDEAIELALHAQEAGADALLVVTPYYNKPTQKGLFAHFSAVAEAVKLPIVIYNIPPRSVVDMSPETMGALVKAHKNIIGVKDATGKLDRVSEQRISCGKDFVQLSGEDGTALGFNAHGGVGCISVTANVAPRLCSEFQAAMLAGDYAKALEYQDRLMPLHRAIFMEPGVCGTKYALSKTRGGNRRVRSPLMSTLEPATEAAIDAALKHAGLMN
>metacyc__BSU16770-MONOMER 4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7) (Bacillus subtilis (strain 168))
MNFGNVSTAMITPFDNKGNVDFQKLSTLIDYLLKNGTDSLVVAGTTGESPTLSTEEKIALFEYTVKEVNGRVPVIAGTGSNNTKDSIKLTKKAEEAGVDAVMLVTPYYNKPSQEGMYQHFKAIAAETSLPVMLYNVPGRTVASLAPETTIRLAADIPNVVAIKEASGDLEAITKIIAETPEDFYVYSGDDALTLPILSVGGRGVVSVASHIAGTDMQQMIKNYTNGQTANAALIHQKLLPIMKELFKAPNPAPVKTALQLRGLDVGSVRLPLVPLTEDERLSLSSTISEL
>ecocyc__DIHYDRODIPICSYN-MONOMER 4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7) (Escherichia coli K-12 substr. MG1655)
MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIKEATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL
>biolip__5t25A Kinetic, spectral and structural characterization of the slow binding inhibitor acetopyruvate with dihydrodipicolinate synthase from escherichia coli.
HMFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIKEATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL
>PDB_2ats_A Dihydrodipicolinate synthase co-crystallised with (s)-lysine
MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGAN
ATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGI
KEATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLH
NKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL
>PDB_3i7s_A Dihydrodipicolinate synthase mutant - k161a - with the substrate pyruvate bound in the active site.
MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGAN
ATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGI
REATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLH
NKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL
>biolip__4pfmA Shewanella benthica dhdps with lysine and pyruvate
HMINGSIVALITPLNSDGTVDYTSLEKLVEYHITEGTDAIVAVGTTGESATLPISEHIAVVGQTVKFASGRIPVIGGNGANATAEAIELTKAQNKLGVAAMLGVTPYYNKPSPKGLIAHYTAVAASTDIPQILYNVPGRTAVDMLPETIAQLVEVPNIIGVKDATGDVARVKQLRDLCGNDFLLYSGDDATAREFLTLGGDGVISVANNIVPKLFKLMCDAALAGDTQAAMAAEDQIKGLFSALFCEANPIPVKWAAHKMGLISQGDIRLPLTELSTEFHGLLLDAMKNARIEVK
>metacyc__MONOMER-6565 dihydrodipicolinate synthase subunit (EC 4.3.3.7) (Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46))
MNFGNIATAMVTPFDKNENIDFQKLSKLIDYLLNNGTDSLVVAGTTGESPTLSEEEKVALIQYSVKEAAGRAPIIAGTGSNNTKASIKLTKKAEEAGADAVMLVTPYYNKPSQEGMYRHFRAIAEETSLPVMLYNVPGRTAASLAPETTIRLAEIPNIIAIKEASGDLDAITKIVAETPEDFAVYSGDDSLTLPALSVGARGIVSVASHIIGPEMQEMIKHYTEGNTAQAALIHQKLLPLMKGLFAAPNPSPLKTALQLKGLDVGSVRLPLIPLNEDERLRLSSLMNGL
>biolip__7lvlA Dihydrodipicolinate synthase bound with allosteric inhibitor (s)- lysine from candidatus liberibacter solanacearum
MFQRSIPALITPFTKDNLIDEDSFVDHIEWQISEGSSGLVPAGTTGESSTLSYEEHCRVVELCVKTAAGRVPVMAGAGSNNTKESIELAQYAQNTGADALLVVVPYYNKPNKKGLLAHFGSIANAVSLPIYIYNNPSRTVIEMDVDTMAELVKTYSNIVGVKDATGRIELASGQRIACGSDFIQLSGDDSSALGFNVHGGVGCISVTANVAPRICAEFQKAISEGDYRQALEYQDKLFPLHQALFIEPSISSVKYALSRLGRNVSLVVRAPMVSILEKETMFAIDQALDHIGLCAG
>PDB_7mjf_A Crystal structure of candidatus liberibacter solanacearum dihydrodipicolinate synthase with pyruvate and succinic semi-aldehyde bound in active site
MFQRSIPALITPFTKDNLIDEDSFVDHIEWQISEGSSGLVPAGTTGESSTLSYEEHCRVVELCVKTAAGRVPVMAGAGSN
NTKESIELAQYAQNTGADALLVVVPYYNKPNKKGLLAHFGSIANAVSLPIYIYNNPSRTVIEMDVDTMAELVKTYSNIVG
VKDATGRIELASGQRIACGSDFIQLSGDDSSALGFNVHGGVGCISVTANVAPRICAEFQKAISEGDYRQALEYQDKLFPL
HQALFIEPSISSVKYALSRLGRNVSLVVRAPMVSILEKETMFAIDQALDHIGLCAG
>BRENDA__Q3M723 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8) (Trichormus variabilis)
MGDFGTVLTAMITPFKADGSVNYAVAAELAAHLVDNGTDTLVVCGTTGESPTLSWDEEYNLFVEVLQTVAGKAKVIAGCGSNSTKEAIAATQKAAKIGVHGTLQVVPYYNKPPQAGLYQHFQAIAQACPDLPLLLYNVPGRTGQNLSPETVVRLAEIDNIIGVKEASGNLDQAGEIRRSTPKEFQIYAGDDSLTLPLLAIGAKGVVSVASHLVGNQLQQMIQAFNSGQVTVASDIHLRLLPLFKALFITTNPIPIKQALKLQGWEVGSTRPPLSDADAEVSQKLEAVMKHLNLI
>biolip__5ktlA Dihydrodipicolinate synthase from the industrial and evolutionarily important cyanobacteria anabaena variabilis.
SVGDFGTVLTAMITPFKADGSVNYAVAAELAAHLVDNGTDTLVVCGTTGESPTLSWDEEYNLFVEVLQTVAGKAKVIAGCGSNSTKEAIAATQKAAKIGVHGTLQVVPYYNKPPQAGLYQHFQAIAQACPDLPLLLYNVPGRTGQNLSPETVVRLAEIDNIIGVKEASGNLDQAGEIRRSTPKEFQIYAGDDSLTLPLLAIGAKGVVSVASHLVGNQLQQMIQAFNSGQVTVASDIHLRLLPLFKALFITTNPIPIKQALKLQGWEVGSTRPPLSDADAEVSQKLEAVMKHLNLI
>biolip__5ud6C Crystal structure of dhdps from cyanidioschyzon merolae with lysine bound
KHFFGRVITALVTPFKLTGVEVDYGVAESLAAHLAENGSDAIIVAGTTGESATLTWSEEYELFRVVKSAVAGTKCRVIAGAGSNSTEEAIEATKKSAKLGLDGTLQVVPYYNKPPQQGIMAHFRAIANAAPDLPMMLYNIPGRTGINMTAETSIKLAEMCPNIVALKEASGNLEQFARIRRATSPDFALYSGDDALTLPLLSLGGNGVVSVASHFIGPEIQRMIEHFVDLGNPEEAFRIHCRYMDLFEALFVMANPIPAKAALRLLGWPVGPTRLPLTDITASAEQQLRQAMIAAGLLS
>SwissProt__P9WP25 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
MTTVGFDVAARLGTLLTAMVTPFSGDGSLDTATAARLANHLVDQGCDGLVVSGTTGESPTTTDGEKIELLRAVLEAVGDRARVIAGAGTYDTAHSIRLAKACAAEGAHGLLVVTPYYSKPPQRGLQAHFTAVADATELPMLLYDIPGRSAVPIEPDTIRALASHPNIVGVKDAKADLHSGAQIMADTGLAYYSGDDALNLPWLAMGATGFISVIAHLAAGQLRELLSAFGSGDIATARKINIAVAPLCNAMSRLGGVTLSKAGLRLQGIDVGDPRLPQVAATPEQIDALAADMRAASVLR
>biolip__5j5dA Crystal structure of dihydrodipicolinate synthase from mycobacterium tuberculosis in complex with alpha-ketopimelic acid
VGFDVAARLGTLLTAMVTPFSGDGSLDTATAARLANHLVDQGCDGLVVSGTTGESPTTTDGEKIELLRAVLEAVGDRARVIAGAGTYDTAHSIRLAKACAAEGAHGLLVVTPYYSKPPQRGLQAHFTAVADATELPMLLYDIPGRSAVPIEPDTIRALASHPNIVGVKDAKADLHSGAQIMADTGLAYYSGDDALNLPWLAMGATGFISVIAHLAAGQLRELLSAFGSGDIATARKINIAVAPLCNAMSRLGGVTLSKAGLRLQGIDVGDPRLPQVAATPEQIDALAADMRAASVLR
>ENA__CAA92211.1 dihydrodipicolinate synthase (Prochlorococcus marinus)
MSPVPEISSAPFGRLLTAMVTPFDTAGAVDFALAARLARYLVDQGSDGLIVCGTTGESPTLSWEEQYQLLETVRNAVNGSAKVLPGTGSNSTSEAIHATAKAAEAGADGALVVVPYYNKPPQAGLESHFRAVAQAAPDLPLMLYNIPGRTGCSISPITVQRLMNCSNIVSFKAASGTTNEVTDLRIRCGSRLAIYSGDDGLPLPMLSVGAVGVVSVASHIVGMRLKAMIEAYFAGENSLALSHHEQLQPLFKALFATTNPIPVKAALELIGWPVGAPRSPLLPLENQMKNELMKTISALLQT
>PDB_1xxx_A Crystal structure of dihydrodipicolinate synthase (dapa, rv2753c) from mycobacterium tuberculosis
GFDVAARLGTLLTAMVTPFSGDGSLDTATAARLANHLVDQGCDGLVVSGTTGESPTTTDGEKIELLRAVLEAVGDRARVI
AGAGTYDTAHSIRLAKACAAEGAHGLLVVTPYYSKPPQRGLQAHFTAVADATELPMLLYDIPGRSAVPIEPDTIRALASH
PNIVGVKDAKADLHSGAQIMADTGLAYYSGDDALNLPWLAMGATGFISVIAHLAAGQLRELLSAFGSGDIATARKINIAV
APLCNAMSRLGGVTLSKAGLRLQGIDVGDPRLPQVAATPEQIDALAADMRAASVLR
>PDB_3l21_B The crystal structure of a dimeric mutant of dihydrodipicolinate synthase (dapa, rv2753c) from mycobacterium tuberculosis - dhdps- a204r
FDVAARLGTLLTAMVTPFSGDGSLDTATAARLANHLVDQGCDGLVVSGTTGESPTTTDGEKIELLRAVLEAVGDRARVIA
GAGTYDTAHSIRLAKACAAEGAHGLLVVTPYYSKPPQRGLQAHFTAVADATELPMLLYDIPGRSAVPIEPDTIRALASHP
NIVGVKDAKADLHSGAQIMADTGLAYYSGDDALNLPWLRMGATGFISVIAHLAAGQLRELLSAFGSGDIATARKINIAVA
PLCNAMSRLGGVTLSKAGLRLQGIDVGDPRLPQVAATPEQIDALAADMRAASVLR
>biolip__4fhaA Structure of dihydrodipicolinate synthase from streptococcus pneumoniae,bound to pyruvate and lysine
SYQDLKECKIITAFITPFHEDGSINFDAIPALIEHLLAHHTDGILLAGTTAESPTLTHDEELELFAAVQKVVNGRVPLIAGVGTNDTRDSIEFVKEVAEFGGFAAGLAIVPYYNKPSQEGMYQHFKAIADASDLPIIIYNIPGRVVVELTPETMLRLADHPNIIGVKECTSLANMAYLIEHKPEEFLIYTGEDGDAFHAMNLGADGVISVASHTNGDEMHEMFTAIAESDMKKAAAIQRKFIPKVNALFSYPSPAPVKAILNYMGFEAGPTRLPLVPAPEEDVKRIIKVVVDGDYEATVTGVLRPDY
>biolip__3di1B Crystal structure of the staphylococcus aureus dihydrodipicolinate synthase-pyruvate complex
MTHLFEGVGVALTTPFTNNKVNIEALKTHVNFLLENNAQAIIVNGTTAESPTLTTDEKERILKTVIDLVDKRVPVIAGTGTNDTEKSIQASIQAKALGADAIMLITPYYNKTNQRGLVKHFEAIADAVKLPVVLYNVPSRTNMTIEPETVEILSQHPYIVALKDATNDFEYLEEVKKRIDTNSFALYSGNDDNVVEYYQRGGQGVISVIANVIPKEFQALYDAQQSGLDIQDQFKPIGTLLSALSVDINPIPIKALTSYLGFGNYELRLPLVSLEDTDTKVLRETYDTFKA
>metacyc__MONOMER-6444 dihydropicolinate synthase subunit (EC 4.3.3.7) (Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025))
MSTGLTAKTGVEHFGTVGVAMVTPFTESGDIDIAAGREVAAYLVDKGLDSLVLAGTTGESPTTTAAEKLELLKAVREEVGDRAKLIAGVGTNNTRTSVELAEAAASAGADGLLVVTPYYSKPSQEGLLAHFGAIAAATEVPICLYDIPGRSGIPIESDTMRRLSELPTILAVKDAKGDLVAATSLIKETGLAWYSGDDPLNLVWLALGGSGFISVIGHAAPTALRELYTSFEEGDLVRAREINAKLSPLVAAQGRLGGVSLAKAALRLQGINVGDPRLPIMAPNEQELEALREDMKKAGVL
>SwissProt__Q5HG25 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 (Staphylococcus aureus (strain COL))
MTHLFEGVGVALTTPFTNNKVNIEALKTHVNFLLENNAQAIIVNGTTAESPTLTTDEKERILKTVIDLVDKRVPVIAGTGTNDTEKSIQASIQAKALGADAIMLITPYYNKTNQRGLVKHFEAIADAVKLPVVLYNVPSRTNMTIEPETVEILSQHPYIVALKDATNDFEYLEEVKKRIDTNSFALYSGNDDNVVEYYQRGGQGVISVIANVIPKEFQALYDAQQSGLDIQDQFKPIGTLLSALSVDINPIPIKALTSYLGFGNYELRLPLVSLEDTDTKVLRETYDTFKAGENE
>SwissProt__Q6GH13 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 (Staphylococcus aureus (strain MRSA252))
MTHLFEGVGVALTTPFTNNKVNLEALKAHVNFLLENNAQAIIVNGTTAESPTLTTDEKELILKTVIDLVDKRVPVIAGTGTNDTEKSIQASIQAKALGADAIMLITPYYNKTNQRGLVKHFEAIADAVKLPVVLYNVPSRTNMTIEPETVEILSQHPYIVALKDATNDFEYLEEVKKRIDTNSFALYSGNDDNVVEYYQRGGQGVISVIANVIPKEFQALYDAQQSGLDIQDQFKPIGTLLSALSVDINPIPIKALTSYLGFGNYELRLPLVSLEDTDTKVLREAYDTFKAGENE
>biolip__5ui3C Crystal structure of dhdps from chlamydomonas reinhardtii
STVDRLKKLRLITAIKTPYLANGKFDLPAYDALVSHQIENGVEGLIVGGTTGEGHLMSWDEHVMLIAHTVNAFGDKTAVIGNTGSNSTREALHATEQGFAVGMHASLQINPYYGKTSKAGLLNHFNAVLNEGPAVVYNVPGRTGQDIPDDVVMEICQHSNFLGMKECTGNSRIKNYTSKGVNCWSGNDDESHDARHSNGAVGVISVTSNVIPGLMHKLMHGSPDPQLNADLKELMAWMFCEPNPISLNTALAMCGLARPVFRLPYVPLSRAQREKGAVLLNKVQEHIPGCKSVRVMEDHEFILVGR
>biolip__6vvhBBB thaliana dihydrodipicolinate synthase isoform 1 (dhdps1) in complex with lysine
EDKNRTNTDDIRSLRVITAIKTPYLPDGRFDLQAYDDLVNTQIENGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGRIKVIGNTGSNSTREAIHATEQGFAMGMHGALHINPYYGKTSIEGMNAHFQTVLHMGPTIIYNVPGRTCQDIPPQVIFKLSQNPNMAGVKECVGNNRVEEYTEKGIVVWSGNDDQCHDSRWDHGATGVISVTSNLVPGLMRKLMFEGRNSALNAKLLPLMDWLFQEPNPIGVNTALAQLGVARPVFRLPYVPLPLSKRIEFVKLVKEIGREHFVGDRDVQVLDDDDFILIGRY
>PDB_7mds_A Crystal structure of atdhdps1 in complex with mbdta-2
NTDDIRSLRVITAIKTPYLPDGRFDLQAYDDLVNTQIENGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGRIKVIG
NTGSNSTREAIHATEQGFAMGMHGALHINPYYGKTSIEGMNAHFQTVLHMGPTIIYNVPGRTCQDIPPQVIFKLSQNPNM
AGVKECVGNNRVEEYTEKGIVVWSGNDDQCHDSRWDHGATGVISVTSNLVPGLMRKLMFEGRNSALNAKLLPLMDWLFQE
PNPIGVNTALAQLGVARPVFRLPYVPLPLSKRIEFVKLVKEIGREHFVGDRDVQVLDDDDFILIGRY
>BRENDA__P24846 4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7) (Triticum aestivum)
MPYLQPPRPHPHPHPTSRLSRASPPSPFPFFPAGTSRSGRLQPVPVSGHSASRVSKGKFAVAAVTLDDYLPMRSTEVKNRTSTDGIKSLRLITAVKTPYLPDGRFDLEAYDSLINTQINGGAEGVIVGGTTGEGHLMSWDEHIMLIGHTVNCFGANIKVIGNTGSNSTREAVHATEQGFAVGMHAALHVNPYYGKTSTEGLISHFKEVLPMGPTIIYNVPSRTSQDIPPPVIEALSSYSNMAGVKECVGHERVKCYTDKGISIWSGNDDECHDSRWKYGATGVISVASNLVPGLMHSLMFEGENAALNEKLLPLMKWLFCEPNPIGLNTALAQLGVVRPVFRLPYTPLPLEKRVEFVRIVEAIGRENFVGQKESRVLDDDDFVLISRY
>BRENDA__Q9FVC8 4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7) (Arabidopsis thaliana)
MAALKGYGLCSMDSALQFPCPKLFNSYKRRSSKWVSPKAAVVPNFHLPMRSLEVKNRTNTDDIKALRVITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTREAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMGPTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGVKECVGNKRVEEYTENGVVVWSGNDDECHDSRWDYGATGVISVTSNLVPGLMRKLMFEGRNSSLNSKLLPLMAWLFHEPNPIGINTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLVKEIGREHFVGEKDVQALDDDDFILIGRY
>ecocyc__G7911-MONOMER KpLE2 phage-like element; putative 2-dehydro-3-deoxy-D-pentonate aldolase (EC 4.1.2.28) (Escherichia coli K-12 substr. MG1655)
MKKFSGIIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSPSTDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLALQNENIVGIKDTIDSVGHLRTMINTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKLLQLPAIYALETPFVSLIKYSMQCVGLPVETYCLPPILEASEEAKDKVHVLLTAQGILPV
>biolip__4hnnF Dihydrodipicolinate synthase from the common grapevine with pyruvate and lysine
HLPMRSFEVKNRTSVDDIKSLRLITAIKTPYLPDGRFDLEAYDALVNMQIVDGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTREAIHATEQGFAVGMHAALHINPYYGKTSLEGLVSHFESVLPMGPTVIYNVPSRTGQDIPPGVIHTVAQSANLAGVKECVGNDRIKQYTDNRIVVWSGNDDQCHDAKWDYGATGVISVTSNLIPGLMRQLLFKGKNPSLNAKIMPLVNWLFEEPNPIGLNTALAQLGVVRPVFRLPYVPLPLAKRVEFVNIVKEIGRENFVGEKDVKVLDDDDFILVGRY