>WP_013722431.1 NCBI__GCF_000204645.1:WP_013722431.1 MQVAATRKIVVLGTGGTIAGTSSVAGASVGYTAAQIGVRQLLAAVPGLAQAAGGVLEAEQVAQIDSKDMDADVWARLAQRCAAHLADPAVAGIVVTHGTDTLEETAWLLHELLDAAKPVVLTCAMRPATALVPDGPQNLLDAVTLAADPSARGVLVVAAGVVHGAREVGKVHPLRLDAFASGDGGPLGWVEAGQVRWAHGRAPLAQPPSHAALLPALGATAWPRVEIVTSHAGADGALVDWLVEKGARGIVAAATGNGTLHKALEAALARAVAAGVAVRVALRCPQGRMLDVYDAPWQGADGLSPVKARISLMLELMRSP >reanno__BFirm_BPHYT_RS08815 L-asparaginase (EC 3.5.1.1) (Burkholderia phytofirmans PsJN) MNTSTSSSAMPSDEGAMPLLPRIVVLATGGTIAGAAASATNTSGYQAGVIGVEQLLAVVPALSTVARMEREQIASVDSKDMAMPLWTTLAQRINTLLADDEIDGVVVTHGTDTLEETAYLLHLTIKSDKPVVLTAAMRPASALSADGPLNLLNAVTVAAQASARGQGVLVAFNNRIHSARDVVKTSTYAVDAFHSPEIGALGWVQDGRVEFQRGVVRPHTLATEFVIGAQWPHVEIVLSYAGVSRIAVDALVAAGVRGIVVAGTGNGSIHASVQQALADAASQGVAVVRASRVGSGHVMRNGAAADDALGFVSAGSLNPYKARVLLMLALAAGATGPMALQKIFDTY >biolip__2wltA The crystal structure of helicobacter pylori l-asparaginase at 1.4 a resolution LPTIALLATGGTIAGSGASLGSYKSGELGVKELLKAIPSLNKIARIQGEQVSNIGSQDMNEEIWFKLAQRAQELLDDSRIQGVVITHGTDTLEESAYFLNLVLHSTKPVVLVGAMRNASSLSADGALNLYEAVSVAVNEKSANKGVLVVMDDTIFSVREVVKTHTTHVSTFKALNSGAIGSVYYGKTRYYMQPLRKHTTESEFSLSQLKTPLPKVDIIYTHAGMTPDLFQASLNSHAKGVVIAGVGNGNVSAGFLKAMQEASQMGVVIVRSSRVGSGGVTSGEIDDKAYGFITSDNLNPQKARVLLQLALTKTNDKAKIQEMFEEY >BRENDA__Q9ZLB9 asparaginase (EC 3.5.1.1) (Helicobacter pylori J99) MAQNLPTIALLATGGTIAGSGVDASLGSYKSGELGVKELLKAIPSLNKIARIQGEQVSNIGSQDMNEEIWFKLAQRAQELLDDSRIQGVVITHGTDTLEESAYFLNLVLHSTKPVVLVGAMRNASSLSADGALNLYYAVSVAVNEKSANKGVLVVMDDTIFRVREVVKTHTTHISTFKALNSGAIGSVYYGKTRYYMQPLRKHTTESEFSLSQLKTPLPKVDIIYTHAGMTPDLFQASLNSHAKGVVIAGVGNGNVSAGFLKAMQEASQMGVVIVRSSRVGSGGVTSGEIDDKAYGFITSDNLNPQKARVLLQLALTKTNDKAKIQEMFEEY >BRENDA__Q6Q4F3 asparaginase (EC 3.5.1.1) (Dickeya chrysanthemi) MERWFKSLFIIAFFFISTANAADKLPNIVILATGGTIAGSAATGTQTTGYKAGALGVDTLINAVPEVKKLANVKGEQFANMASENMTGDVVLKLSQRVNALLARDDVDGVVITHGTDTLEESAYFLHLTVKSDKPVVFAAAMRPATAISADGPMNLLEAVRVASDKQSRGRGVLVVLNDRIGSARYITKSNASTLDSFRANEEGYLGVVIGNHIYYQNRLDKLHTNRSVFDVRGLASLPKVDILYGYQDDSEYLYDAAISHGVKGIVYAGMGAGSVSVRGIAGMRKAQDKGVVVMRSSRTGNGIVPPDEALPGLVADSLNPAHARILLMLALTRTSDPAVIQDYFHTY >PDB_1hg0_A X-ray structure of the complex between erwinia chrysanthemi l- asparaginase and succinic acid ADKLPNIVILATGGTIAGSAATGTQTTGYKAGALGVDTLINAVPEVKKLANVKGEQFSNMASENMTGDVVLKLSQRVNEL LARDDVDGVVITHGTDTVEESAYFLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGRGVMVVINDRI GSARYITKTNASTLDTFRANEEGYLGVIIGNRIYYQNRIDKLHTTRSVFDVRGLTSLPKVDILYGYQDDPEYLYDAAIQH GVKGIVYAGMGAGSVSVRGIAGMRKALEKGVVVMRSTRTGNGIVPPDEELPGLVSDSLNPAHARILLMLALTRTSDPKVI QEYFHTY >PDB_1jsr_A Crystal structure of erwinia chrysanthemi l-asparaginase complexed with 6-hydroxy-l-norleucine LPNIVILATGGTIAGSAATGTQTTGYKAGALGVDTLINAVPEVKKLANVKGEQFSNMASENMTGDVVLKLSQRVNELLAR DDVDGVVITHGTDTVEESAYFLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGRGVMVVINDRIGSA RYITKTNASTLDTFRANEEGYLGVIIGNRIYYQNRIDKLHTTRSVFDVRGLTSLPKVDILYGYQDDPEYLYDAAIQHGVK GIVYAGMGAGSVSVRGIAGMRKALEKGVVVMRSTRTGNGIVPPDEELPGLVSDSLNPAHARILLMLALTRTSDPKVIQEY FHTY >PDB_1jsl_A Crystal structure of erwinia chrysanthemi l-asparaginase complexed with 6-hydroxy-d-norleucine LPNIVILATGGTIAGSAATGTQTTGYKAGALGVDTLINAVPEVKKLANVKGEQFSNMASENMTGDVVLKLSQRVNELLAR DDVDGVVITHGTDTVEESAYFLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGRGVMVVINDRIGSA RYITKTNASTLDTFRANEEGYLGVIIGNRIYYQNRIDKLHTTRSVFDVRGLTSLPKVDILYGYQDDPEYLYDAAIQHGVK GIVYAGMGAGSVSVRGIAGMRKALEKGVVVMRSTRTGNGIVPPDEELPGLVSDSLNPAHARILLMLALTRTSDPKVIQEY FHTY >SwissProt__P06608 L-asparaginase; L-ASNase; L-asparagine amidohydrolase; EC 3.5.1.1 (Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)) MERWFKSLFVLVLFFVFTASAADKLPNIVILATGGTIAGSAATGTQTTGYKAGALGVDTLINAVPEVKKLANVKGEQFSNMASENMTGDVVLKLSQRVNELLARDDVDGVVITHGTDTVEESAYFLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGRGVMVVLNDRIGSARYITKTNASTLDTFKANEEGYLGVIIGNRIYYQNRIDKLHTTRSVFDVRGLTSLPKVDILYGYQDDPEYLYDAAIQHGVKGIVYAGMGAGSVSVRGIAGMRKAMEKGVVVIRSTRTGNGIVPPDEELPGLVSDSLNPAHARILLMLALTRTSDPKVIQEYFHTY >BRENDA__B6ZCD8 asparaginase (EC 3.5.1.1) (Helicobacter pylori) MAQNLPTIALLATGGTIAGSGASASSDSYKSGELGIKELLKAIPSLNKIARIQGEQVSNIGSQDMNEEIWFKLAKRAQELLDDSRIQGVVITHGTDTLEESAYFLNLVLRSTKPVVLVGAMRNAASLSADGALNLYNALSVALNEKSANKGVLVVMDDTIFSAREVVKTHTTHTSTFKALNSGAIGSVYYGKVRYYMQPLRKHTTESEFSILELKTPLPKVDIIYTHASMTSDLFQASLKSHAKGVVIAGVGNGNVSAGFLKTMQEAGQMGVVIVRSSRVGSGEITSGEIDDKTFITSDNLNPQKARVLLQLALTKTNDKAKIQEMFEEY >metacyc__STM3598-MONOMER N-(1-deoxy-D-fructos-1-yl)-L-asparaginase (EC 3.5.1.1) (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)) MKIRVFMATVLLLISHCVFSTTSLPHIVILATGGTIAGTAANNTQTAGYKSGELGVQTLINAVPEMNNIARVDGEQVANIGSENMTSDIILKLSQKVNALLARDDVDGVVITHGTDTLDETAYFLNLTVKSDKPVVFTAAMRPASAISADGAMNLLEAVTVAADPNAKGRGVMVVLNDRIGSARFVTKTNATTLDTFKAPEEGYLGVIVNGQPQFETRVEKIHTLRSVFDVRNIKKLPNVVIIYGYQDDPEYMYDAAIAHHADGIIYAGTGAGSVSVRSDAGIKKAEKAGIIVVRASRTGNGVVPLDKGQPGLVSDSLNPAKARVLLMTALTQTRNPELIQSYFSTY >biolip__5k3oA Wolinella succinogenes l-asparaginase p121 and l-aspartic acid KPQVTILATGGTIAGSGESSVKSSYSAGAVTVDKLLAAVPAINDLATIKGEQISSIGSQEMTGKVWLKLAKRVNELLAQKETEAVIITHGTDTMEETAFFLNLTVKSQKPVVLVGAMRPGSSMSADGPMNLYNAVNVAINKASTNKGVVIVMNDEIHAAREATKLNTTAVNAFASPNTGKIGTVYYGKVEYFTQSVRPHTLASEFDISKIEELPRVDILYAHPDDTDVLVNAALQAGAKGIIHAGMGNGNPFPLTQNALEKAAKSGVVVARSSRVGSGSTTQEAEVDDKKLGFVATESLNPQKARVLLMLALTKTSDREAIQKIFSTY >PDB_5k45_A Wolinella succinogenes l-asparaginase p121 + l-glutamic acid KPQVTILATGGTIAGSGESSVKSSYSAGAVTVDKLLAAVPAINDLATIKGEQISSIGSQEMTGKVWLKLAKRVNELLAQK ETEAVIITHGTDTMEETAFFLNLTVKSQKPVVLVGAMRPGSSMSADGPMNLYNAVNVAINKASTNKGVVIVMNDEIHAAR EATKLNTTAVNAFASPNTGKIGTVYYGKVEYFTQSVRPHTLASEFDISKIEELPRVDILYAHPDDTDVLVNAALQAGAKG IIHAGMGNGNPFPLTQNALEKAAKSGVVVARSSRVGSGSTTQEAEVDDKKLGFVATESLNPQKARVLLMLALTKTSDREA IQKIFSTY >biolip__7u6mC Albumin binding domain fused to a mutant of the erwinia asparaginase IEDICLPRWGCLWEDDDKLPNIVILATGGTIAGSAATGTQTTGYKIGALGVDTLINAVPEVKKLANVKGEQFSNMASQNMTGDVVLKLSQRVNELLARDDVDGVVITHGTDTVEESAYFLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGRGVMVVLNDRIGSARYITKTNASTLDTFKANEEGYLGVIIGNRIYYQNRIDKLHTTRSVFDVRGLTSLPKVDILYGYQDDPEYLYDAAIQHGVKGIVYAGMGAGQVSVRGIAGMRKAMEKGVVVIRSTRTGNGIVPPDEELPGLVSDSLNPAHARILLMLALTRTSDPKVIQEYFHTY >BRENDA__P50286 asparaginase (EC 3.5.1.1) (Wolinella succinogenes) MAKPQVTILATGGTIAGSGESSVKSSYSAGAVTVDKLLAAVPAINDLATIKGEQISSIGSQEMTGKVWLKLAKRVNELLAQKETEAVIITHGTDTMEETAFFLNLTVKSQKPVVLVGAMRSGSSMSADGPMNLYNAVNVAINKASTNKGVVIVMNDEIHAAREATKLNTTAVNAFASPNTGKIGTVYYGKVEYFTQSVRPHTLASEFDISKIEELPRVDILYAHPDDTDVLVNAALQAGAKGIIHAGMGNGNPFPLTQNALEKAAKSGVVVARSSRVGSGSTTQEAEVDDKKLGFVATESLNPQKARVLLMLALTKTSDREAIQKIFSTY >BRENDA__Q66CJ2 asparaginase (EC 3.5.1.1) (Yersinia pseudotuberculosis) MKYIKLTVLAGIFVGISSPVFALPNITLLATGGTIAGGGDSATKSNYTAGKLGVDALVEAVPAIKDIANIQGEQVVNIGSQDMNDDVWLTLAKKINKDCTKTDGFVITHGTDTLEETAYFLDLTVNCDKPVVIVGAMRPATALGADGPLNLYNAVVVASEADSAKRGVLVAMNDMVFTGRDVVKTNTTSVQTFQSPNTGPLGYIYDGKVNYLHQPAARQPAFDISKLNTLPKVGIIYNYANASDIPAKALIADGYQGIVSAGVGNGNLYHTVFDTLATAASHGVAVVRSSRVPSGSTTEGAEIDDAKYGFVAAGALNPQKARVLLQLALTQTQKPQEIQKLFHTY >metacyc__MONOMER-13049 L-asparaginase subunit (EC 3.5.1.38) (Pectobacterium atrosepticum) MFNALFVVVFVCFSSLANAAENLPNIVILATGGTIAGSAAANTQTTGYKAGALGVETLIQAVPELKTLANIKGEQVASIGSENMTSDVLLTLSKRVNELLARSDVDGVVITHGTDTLDESPYFLNLTVKSDKPVVFVAAMRPATAISADGPMNLYGAVKVAADKNSRGRGVLVVLNDRIGSARFISKTNASTLDTFKAPEEGYLGVIIGDKIYYQTRLDKVHTTRSVFDVTNVDKLPAVDIIYGYQDDPEYMYDASIKHGVKGIVYAGMGAGSVSKRGDAGIRKAESKGIVVVRSSRTGSGIVPPDAGQPGLVADSLSPAKSRILLMLALTKTTNPAVIQDYFHAY >biolip__2gvnA L-asparaginase from erwinia carotovora in complex with aspartic acid NLPNIVILATGGTIAGSAAANTQTTGYKAGALGVETLIQAVPELKTLANIKGEQVASIGSENMTSDVLLTLSKRVNELLARSDVDGVVITHGTDTLDESPYFLNLTVKSDKPVVFVAAMRPATAISADGPMNLYGAVKVAADKNSRGRGVLVVLNDRIGSARFISKTNASTLDTFKAPEEGYLGVIIGDKIYYQTRLDKVHTTRSVFDVTNVDKLPAVDIIYGYQDDPEYMYDASIKHGVKGIVYAGMGAGSVSKRGDAGIRKAESKGIVVVRSSRTGSGIVPPDAGQPGLVADSLSPAKSRILLMLALTKTTNPAVIQDYFHAY >BRENDA__A0A2X5A091 asparaginase (EC 3.5.1.1); glutaminase (EC 3.5.1.2) (Helicobacter pylori) MRIFLKLLILLFCLKGQVMAQNLPTIALLATGGTIAGSSASASLGSYKSGELGIKDILKAVPSLNKIARIQGEQISNIGSQDMNEEVWFKLAKRAQELLDDSRIQGVVITHGTDTLEESAYFLNLVLRSTKPVVLVGAMRNAASLSADGALNLYNALSVATNEKSANKGVLVVMDDNIFSAREVVKTHTTHTSTFKALNSGAIGSVYYGKARYYMQPLRKHTIESEFSILELNPPLPKVDIIYTHVGMTPDLFQASLNSHAKGVVIAGVGNGNVSAGLLKAMQEASQMGVVIVRSSRVGSGEITSGEIDDKAFITSDNLNPQKARVLLQLALTKTNDKAKIQEMFEEY >BRENDA__C0KWF5 asparaginase (EC 3.5.1.1) (Escherichia coli) MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTAGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDDVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKTVFDTLATAAKNGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY >ecocyc__ANSB-MONOMER L-asparaginase 2 (EC 3.5.1.38; EC 3.5.1.1) (Escherichia coli K-12 substr. MG1655) MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY >PDB_1ho3_A Crystal structure analysis of e. Coli l-asparaginase ii (y25f mutant) LPNITILATGGTIAGGGDSATKSNFTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKT DGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDV TKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIV SAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQ QIFNQY >SwissProt__O34482 L-asparaginase 2; L-ASNase 2; L-asparagine amidohydrolase 2; EC 3.5.1.1 (Bacillus subtilis (strain 168)) MKKQRMLVLFTALLFVFTGCSHSPETKESPKEKAQTQKVSSASASEKKDLPNIRILATGGTIAGADQSKTSTTEYKAGVVGVESLIEAVPEMKDIANVSGEQIVNVGSTNIDNKILLKLAKRINHLLASDDVDGIVVTHGTDTLEETAYFLNLTVKSDKPVVIVGSMRPSTAISADGPSNLYNAVKVAGAPEAKGKGTLVVLNDRIASARYVTKTNTTTTDTFKSEEMGFVGTIADDIYFNNEITRKHTKDTDFSVSNLDELPQVDIIYGYQNDGSYLFDAAVKAGAKGIVFAGSGNGSLSDAAEKGADSAVKKGVTVVRSTRTGNGVVTPNQDYAEKDLLASNSLNPQKARMLLMLALTKTNDPQKIQAYFNEY >PDB_1jaz_A Crystal structure of monoclinic form of d90e mutant of escherichia coli asparaginase ii LPNITILATGGTIAGLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTETMEETAYFL DLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPL GYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLAT AAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY >PDB_7r5q_A Escherichia coli type ii asparaginase n24s mutant in complex with glu LPNITILATGGTIAGVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD LTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLG YIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATA AKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY >PDB_1hg1_A X-ray structure of the complex between erwinia chrysanthemi l- asparaginase and d-aspartate LPNIVILATGGTIGVDTLINAVPEVKKLANVKGEQFSNMASENMTGDVVLKLSQRVNELLARDDVDGVVITHGTDTVEES AYFLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGRGVMVVINDRIGSARYITKTNASTLDTFRANE EGYLGVIIGNRIYYQNRIDKLHTTRSVFDVRGLTSLPKVDILYGYQDDPEYLYDAAIQHGVKGIVYAGMGAGSVSVRGIA GMRKALEKGVVVMRSTRTGNGIVPPDEELPGLVSDSLNPAHARILLMLALTRTSDPKVIQEYFHTY >PDB_1hfw_A X-ray structure of the complex between erwinia chrysanthemi l- asparaginase and l-glutamate KLPNIVILATGGTIAVDTLINAVPEVKKLANVKGEQFSNMASENMTGDVVLKLSQRVNELLARDDVDGVVITHGTDTVEE SAYFLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGRGVMVVINDRIGSARYITKTNASTLDTFRAN EEGYLGVIIGNRIYYQNRIDKLHTTRSVFDVRGLTSLPKVDILYGYQDDPEYLYDAAIQHGVKGIVYAGMGAGSVSVRGI AGMRKALEKGVVVMRSTRTGNGIVPPDEELPGLVSDSLNPAHARILLMLALTRTSDPKVIQEYFHTY >biolip__6pa3A E. Coli l-asparaginase ii double mutant (t89v,k162t) in complex with l-asn at ph 7.0 MDHHHHHHLPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGVDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTTTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY >PDB_2hln_A L-asparaginase from erwinia carotovora in complex with glutamic acid NLPNIVILATGGTIAGVETLIQAVPELKTLANIKGEQVASIGSENMTSDVLLTLSKRVNELLARSDVDGVVITHGTDTLD ESPYFLNLTVKSDKPVVFVAAMRPATAISADGPMNLYGAVKVAADKNSRGRGVLVVLNDRIGSARFISKTNASTLDTFKA PEEGYLGVIIGDKIYYQTRLDKVHTTRSVFDVTNVDKLPAVDIIYGYQDDPEYMYDASIKHGVKGIVYAGMGAGSVSKRG DAGIRKAESKGIVVVRSSRTGSGIVPPDAGQPGLVADSLSPAKSRILLMLALTKTTNPAVIQDYFHAY >PDB_6wyw_A Crystal structure of pseudomonas 7a glutaminase-asparaginase in complex with l-asp at ph 4.5 LANVVILATGGTIAGAAKLGVDKLIAGVPELADIANVRGEQVMQIASESISNDDLLKLGKRVAELAESKDVDGIVITHGT DTLEETAFFLNLVEKTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASDKQSRGKGVLVTMNDEIQSGRDVSKAVNIKTE AFKSAWGPMGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYGYGNVTDTAYKALAQNGAKALIHAGTGNGSVS SRVVPALQELRKNGVQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPQKARILAMVAMTKTQDSKELQRIFWEY >SwissProt__O68897 Glutaminase-asparaginase; L-ASNase/L-GLNase; L-asparagine/L-glutamine amidohydrolase; EC 3.5.1.38 (Pseudomonas fluorescens biotype A) MKSALKTFVPGALALLLLFPVAAQAKEVETKTKLANVVILATGGTIAGAGASAANSATYQAAKVGIEQLIAGVPELSQIANVRGEQVMQIASESINNENLLQLGRRVAELADSKDVDGIVITHGTDTLEETAYFLNLVEKTDKPIIVVGSMRPGTAMSADGMLNLYNAVAVAGSKDARGKGVLVTMNDEIQSGRDVSKMINIKTEAFKSPWGPLGMVVEGKSYWFRLPAKRHTMDSEFDIKTIKSLPDVEIAYGYGNVSDTAVKALAQAGAKAIIHAGTGNGSVSSKVVPALQELRKQGVQIIRSSHVNAGGFVLRNAEQPDDKYDWVVAHDLNPQKARILAMVALTKTQDSKELQRMFWEY >SwissProt__P10182 Glutaminase-asparaginase; L-ASNase/L-GLNase; L-asparagine/L-glutamine amidohydrolase; PGA; EC 3.5.1.38 (Pseudomonas sp. (strain ATCC 29598 / 7A)) KEVENQQKLANVVILATGGTIAGAGASAANSATYQAAKVGVDKLIAGVPELADLANVRGEQVMQIASESITNDDLLKLGKRVAELADSNDVDGIVITHGTDTLEETAYFLDLTLNTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASNKDSRGKGVLVTMNDEIQSGRDVSKSINIKTEAFKSAWGPLGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYSYGNVTDTAYKALAQNGAKALIHAGTGNGSVSSRLTPALQTLRKTGTQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPEKARILVELAMVKTQDSKELQRIFWEY >PDB_6wyy_A Crystal structure of pseudomonas 7a glutaminase-asparaginase in complex with l-glu at ph 6.5 KLANVVILATGGTIAGLGVDKLIAGVPELADIANVRGEQVMQIASESISNDDLLKLGKRVAELAESKDVDGIVITHGTDT LEETAFFLNLVEKTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASDKQSRGKGVLVTMNDEIQSGRDVSKAVNIKTEAF KSAWGPMGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYGYGNVTDTAYKALAQNGAKALIHAGTGNGSVSSR VVPALQELRKNGVQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPQKARILAMVAMTKTQDSKELQRIFWEY >biolip__1djoA Crystal structure of pseudomonas 7a glutaminase-asparaginase with the inhibitor donv covalently bound in the active site KLANVVILATGGTIAGAGASAANSATYQAAKVGVDKLIAGVPELADLANVRGEQVMQIASESITNDDLLKLGKRVAELADSNDVDGIVITHGTDTLEETAYFLNLVQKTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASNKDSRGKGVLVTMNDEIQSGRDVSKSINIKTEAFKSAWGPLGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYSYGNVTDTAYKALAQNGAKALIHAGTGNGSVSSRVVPALQQLRKNGTQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPEKARILAMVAMTKTQDSKELQRIFWEY >PDB_4pga_A Glutaminase-asparaginase from pseudomonas 7a KLANVVILATGGTIAGAGASAANSATYQAAKVGVDKLIAGVPELADLANVRGEQVMQIASESITNDDLLKLGKRVAELAD SNDVDGIVITHGTDTLEETAYFLNLVQKTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASNKDSRGKGVLVTMNDEIQS GRDVSKSINIKTEAFKSAWGPLGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYSYGNVTDTAYKALAQNGAK ALIHAGTGNGSVSSRVVPALQQLRKNGTQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPEKARILAMVAMTKTQDS KELQRIFWEY >PDB_1djp_A Crystal structure of pseudomonas 7a glutaminase-asparaginase with the inhibitor don covalently bound in the active site KLANVVILATGGTIAGAGASAANSATYQAAKVGVDKLIAGVPELADLANVRGEQVMQIASESITNDDLLKLGKRVAELAD SNDVDGIVITHGTDTLEETAYFLNLVQKTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASNKDSRGKGVLVTMNDEIQS GRDVSKSINIKTEAFKSAWGPLGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYSYGNVTDTAYKALAQNGAK ALIHAGTGNGSVSSRVVPALQQLRKNGTQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPEKARILAMVAMTKTQDS KELQRIFWEY >CharProtDB__CH_006653 glutaminase-asparaginase; EC 3.5.1.38 (Acinetobacter glutaminasificans) KNNVVIVATGGTIAGAGASSTNSATYSAAKVPVDALIKAVPQVNDLANITGIQALQVASESITDKELLSLARQVNDLVKKPSVNGVVITHGTDTMEETAFFLNLVVHTDKPIVLVGSMRPSTALSADGPLNLYSAVALASSNEAKNKGVMVLMNDSIFAARDVTKGINIHTHAFVSQWGALGTLVEGKPYWFRSSVKKHTNNSEFNIEKIQGDALPGVQIVYGSDNMMPDAYQAFAKAGVKAIIHAGTGNGSMANYLVPEVRKLHDEQGLQIVRSSRVAQGFVLRNAEQPDDKYGWIAAHDLNPQKARLLMALALTKTNDAKEIQNMFWNY >PDB_6wyz_A Crystal structure of pseudomonas 7a glutaminase-asparaginase (mutant k173m) in complex with d-glu at ph 5.5 LANVVILATGGTIAGVDKLIAGVPELADIANVRGEQVMQIASESISNDDLLKLGKRVAELAESKDVDGIVITHGTDTLEE TAFFLNLVEKTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASDKQSRGKGVLVTMNDEIQSGRDVSMAVNIKTEAFKSA WGPMGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYGYGNVTDTAYKALAQNGAKALIHAGTGNGSVSSRVVP ALQELRKNGVQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPQKARILAMVAMTKTQDSKELQRIFWEY >BRENDA__P38986 asparaginase (EC 3.5.1.1) (Saccharomyces cerevisiae) MKSDSVEITTICPDVENSQFVVQSNCPETIPEILKSQNAAVNGSGIACQQRSLPRIKILGTGGTIASKAIDSSQTAGYHVDLTIQDLLDAIPDISKVCDIEYEQLCNVDSKDINEDILYKIYKGVSESLQAFDGIVITHGTDTLSETAFFIESTIDAGDVPIVFVGSMRPSTSVSADGPMNLYQAICIASNPKSRGRGVLVSLNDQISSGYYITKTNANSLDSFNVRQGYLGNFVNNEIHYYYPPVKPQGCHKFKLRVDGKHFKLPEVCILYAHQAFPPAIVNLVADKYDGIVLATMGAGSLPEEVNETCMKLSLPIVYSKRSMDGMVPIANVPKKGSKEDNLIASGYLSPEKSRILLQLCLAGNYTLEEIKHVFTGVYGG >SwissProt_P38986 L-asparaginase 1; L-asparaginase I; L-asparagine amidohydrolase I; ASP I; EC 3.5.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) MKSDSVEITTICPDVENSQFVVQSNCPETIPEILKSQNAAVNGSGIACQQRSLPRIKILGTGGTIASKAIDSSQTAGYHV DLTIQDLLDAIPDISKVCDIEYEQLCNVDSKDINEDILYKIYKGVSESLQAFDGIVITHGTDTLSETAFFIESTIDAGDV PIVFVGSMRPSTSVSADGPMNLYQAICIASNPKSRGRGVLVSLNDQISSGYYITKTNANSLDSFNVRQGYLGNFVNNEIH YYYPPVKPQGCHKFKLRVDGKHFKLPEVCILYAHQAFPPAIVNLVADKYDGIVLATMGAGSLPEEVNETCMKLSLPIVYS KRSMDGMVPIANVPKKGSKEDNLIASGYLSPEKSRILLQLCLAGNYTLEEIKHVFTGVYGG >SwissProt__P0CX77 L-asparaginase 2-2; L-asparaginase II; L-asparagine amidohydrolase II; ASP II; EC 3.5.1.1 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)) MRSLNTLLLSLFVAMSSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTDPSEIPEVIILYSYQGLNPELIVKAVKDLGAKGIVLAGSGAGSWTATGSIVNEQLYEEYGIPIVHSRRTADGTVPPDDAPEYAIGSGYLNPQKSRILLQLCLYSGYGMDQIRSVFSGVYGG