ID A8FIX4_BACP2 Unreviewed; 473 AA. AC A8FIX4; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 04-NOV-2026, entry version 97. 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 Name=aspA {ECO:0000313|EMBL:ABV64191.1}; GN OrderedLocusNames=BPUM_3547 {ECO:0000313|EMBL:ABV64191.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV64191.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV64191.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV64191.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). RN [2] {ECO:0000313|EMBL:ABV64191.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV64191.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=23812891; DOI=10.1007/s00792-013-0559-z; RA Tirumalai M.R., Fox G.E.; RT "An ICEBs1-like element may be associated with the extreme radiation and RT desiccation resistance of Bacillus pumilus SAFR-032 spores."; RL Extremophiles 17:767-774(2013). RN [3] {ECO:0000313|EMBL:ABV64191.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV64191.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=23799069; RA Tirumalai M.R., Rastogi R., Zamani N., O'Bryant Williams E., Allen S., RA Diouf F., Kwende S., Weinstock G.M., Venkateswaran K.J., Fox G.E.; RT "Candidate genes that may be responsible for the unusual resistances RT exhibited by Bacillus pumilus SAFR-032 spores."; RL PLoS ONE 8:E66012-E66012(2013). 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; CP000813; ABV64191.1; -; Genomic_DNA. DR RefSeq; WP_012011744.1; NC_009848.4. DR STRING; 315750.BPUM_3547; -. DR PaxDb; 315750-BPUM_3547; -. DR GeneID; 5622836; -. DR KEGG; bpu:BPUM_3547; -. DR eggNOG; COG1027; Bacteria. DR HOGENOM; CLU_021594_4_1_9; -. DR OMA; AAAQCMF; -. DR OrthoDB; 9802809at2; -. 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; IPR022761; Fumarate-Lyase-like_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR008948; L-Aspartase-like. 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 NCBIfam; TIGR00839; aspA; 1. DR NCBIfam; NF008909; PRK12273.1; 1. DR NCBIfam; NF011092; PRK14515.1; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. 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 Proteomes; UP000001355; Chromosome. DR AlphaFoldDB; A8FIX4; -. PE 3: Inferred from homology; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362017}; KW Reference proteome {ECO:0000313|Proteomes:UP000001355}. FT DOMAIN 15..343 FT /note="Fumarate lyase-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00206" FT DOMAIN 410..462 FT /note="Fumarase C C-terminal" FT /evidence="ECO:0000259|Pfam:PF10415" SQ SEQUENCE 473 AA; 52249 MW; D668A042A4D54582 CRC64; MVQATYRYEK DFLGEKEILA DVYYGVQTLR AKENFPITGY RMHEELIRAF AIVKKAAAQA NMEVGRLYEG IGNAIVQASD EVIEGKLHEY FIVDPIQGGA GTSMNMNANE VIGNRALEIM GHQKGEYIHL SPNTHVNMSQ STNDSFPTAI HIAVLKQLDI LLETMQTMQD VFQKKAKEFD HVIKMGRTHL QDAVPIRLGQ EFEAYSRVLS RDIKRINQSK QHLYEVNMGA TAVGTGLNAD PRYIEIVVKK LADISGLPLV GAEHLVDATQ NTDAYTEVSA ALKVCMMNMS KIANDLRLMA SGPRAGLAEI ALPARQPGSS IMPGKVNPVM AELINQIAFQ VIGNDHTICL ASEAGQLELN VMEPVLVFNL LQSISIMNNG FRSFTDHCLV DIEANEKRLK EYVEKSAGVI TAVNPHLGYE AAARIAREAI LTGQSIRDLC LQNDVLTEEE LDIILNPFEM TKPGIAGAEL LER //