ID A7GL70_BACCN Unreviewed; 477 AA. AC A7GL70; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 02-SEP-2026, entry version 111. DE RecName: Full=Aspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00016146, ECO:0000256|NCBIfam:TIGR00839}; DE Short=Aspartase {ECO:0000256|RuleBase:RU362017}; DE EC=4.3.1.1 {ECO:0000256|ARBA:ARBA00012992, ECO:0000256|NCBIfam:TIGR00839}; GN OrderedLocusNames=Bcer98_0526 {ECO:0000313|EMBL:ABS20878.1}; OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS20878.1, ECO:0000313|Proteomes:UP000002300}; RN [1] {ECO:0000313|EMBL:ABS20878.1, ECO:0000313|Proteomes:UP000002300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98 RC {ECO:0000313|Proteomes:UP000002300}; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.H., Sanchis V., RA Nguen-The C., Lereclus D., Richardson P., Wincker P., Weissenbach J., RA Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate = fumarate + NH4(+); Xref=Rhea:RHEA:16601, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29806, ChEBI:CHEBI:29991; EC=4.3.1.1; CC Evidence={ECO:0000256|ARBA:ARBA00001494, CC ECO:0000256|RuleBase:RU362017}; CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. CC Aspartase subfamily. {ECO:0000256|ARBA:ARBA00005596, CC ECO:0000256|RuleBase:RU362017}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000764; ABS20878.1; -; Genomic_DNA. DR RefSeq; WP_011983634.1; NC_009674.1. DR AlphaFoldDB; A7GL70; -. DR STRING; 315749.Bcer98_0526; -. DR PaxDb; 315749-Bcer98_0526; -. DR GeneID; 33895885; -. DR KEGG; bcy:Bcer98_0526; -. DR eggNOG; COG1027; Bacteria. DR HOGENOM; CLU_021594_4_0_9; -. DR OrthoDB; 9802809at2; -. DR Proteomes; UP000002300; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR CDD; cd01357; Aspartase; 1. DR FunFam; 1.10.40.30:FF:000002; Fumarate hydratase class II; 1. DR FunFam; 1.10.275.10:FF:000001; Fumarate hydratase, mitochondrial; 1. DR FunFam; 1.20.200.10:FF:000001; Fumarate hydratase, mitochondrial; 1. DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1. DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1. DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1. DR InterPro; IPR004708; ApsA. DR InterPro; IPR051546; Aspartate_Ammonia-Lyase. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR018951; Fumarase_C_C. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR NCBIfam; TIGR00839; aspA; 1. DR NCBIfam; NF008909; PRK12273.1; 1. DR NCBIfam; NF011092; PRK14515.1; 1. DR PANTHER; PTHR42696; ASPARTATE AMMONIA-LYASE; 1. DR PANTHER; PTHR42696:SF2; ASPARTATE AMMONIA-LYASE; 1. DR Pfam; PF10415; FumaraseC_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00145; ARGSUCLYASE. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; L-aspartase-like; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362017}; KW Reference proteome {ECO:0000313|Proteomes:UP000002300}. FT DOMAIN 15..344 FT /note="Fumarate lyase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00206" FT DOMAIN 410..463 FT /note="Fumarase C C-terminal" FT /evidence="ECO:0000259|Pfam:PF10415" SQ SEQUENCE 477 AA; 52624 MW; 3E65C8ADA5CD0852 CRC64; MIATKDIRIE KDFLGEKEVP NEAYYGVQTL RAVENFPITG YRIHDSLITA MAIVKKAAAL ANVETGYLPE NIGKEIAAAA QEIMDGKLHD QFIVDPIQGG AGTSINMNAN EVIANRALER MGYEKGDYAK ISPNTHVNMA QSTNDAFPTG IHIATLMMLE ELLITMEELH RAFIKKAKEF DHVIKMGRTH LQDAVPIRLG QEFSAYSRVL ERDIKRIKQS RQHLYEVNMG ATAVGTGLNA NPMYIEQVVK HLRELSGFPL VGAEHLVDAT QNTDAYTEVS AALKVCMMNM SKIANDLRIM ASGPRVGLAE IQLPARQPGS SIMPGKVNPV MAEVINQVAF QVIGNDHTIC LASEAGQLEL NVMEPVLVFN LIQSISIMNN AFRVFREYCI EGITANEELL KEYVERSVGI ITAVNPHIGY EAASRIAREA IATGKSVREL CLEHGVLTEE ELDIILDPYE MTHPEIAGAS LLKNKKS //