ID A0A0D6QLW5_9DELT Unreviewed; 131 AA. AC A0A0D6QLW5; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 22-NOV-2017, entry version 26. DE RecName: Full=Aspartate 1-decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446}; DE EC=4.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00446}; DE AltName: Full=Aspartate alpha-decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446}; DE Contains: DE RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00446}; DE Contains: DE RecName: Full=Aspartate 1-decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00446}; GN Name=panD {ECO:0000256|HAMAP-Rule:MF_00446, GN ECO:0000313|EMBL:GAO04394.1}; GN ORFNames=PSR1_03288 {ECO:0000313|EMBL:GAO04394.1}; OS Anaeromyxobacter sp. PSR-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=1300915 {ECO:0000313|EMBL:GAO04394.1, ECO:0000313|Proteomes:UP000032665}; RN [1] {ECO:0000313|EMBL:GAO04394.1, ECO:0000313|Proteomes:UP000032665} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PSR-1 {ECO:0000313|EMBL:GAO04394.1, RC ECO:0000313|Proteomes:UP000032665}; RX PubMed=23709511; DOI=10.1128/AEM.00693-13; RA Kudo K., Yamaguchi N., Makino T., Ohtsuka T., Kimura K., Dong DT., RA Amachi S.; RT "Release of arsenic from soil by a novel dissimilatory arsenate- RT reducing bacterium, Anaeromyxobacter sp. strain PSR-1."; RL Appl. Environ. Microbiol. 79:4635-4642(2013). RN [2] {ECO:0000313|Proteomes:UP000032665} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PSR-1 {ECO:0000313|Proteomes:UP000032665}; RA Tonomura M., Ehara A., Suzuki H., Amachi S.; RT "Draft Genome Sequence of Anaeromyxobacter sp. Strain PSR-1, an RT Arsenate-Respiring Bacterium Isolated from Arsenic-Contaminated RT Soil."; RL Genome Announc.3:e00472-15(2015). CC -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of CC aspartate to produce beta-alanine. {ECO:0000256|HAMAP- CC Rule:MF_00446, ECO:0000256|SAAS:SAAS00683550}. CC -!- CATALYTIC ACTIVITY: L-aspartate = beta-alanine + CO(2). CC {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00683552}. CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00446, CC ECO:0000256|PIRSR:PIRSR006246-1}; CC Note=Binds 1 pyruvoyl group covalently per subunit. CC {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|PIRSR:PIRSR006246- CC 1}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC beta-alanine from L-aspartate: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_00446, ECO:0000256|SAAS:SAAS00683554}. CC -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits. CC {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00683537}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446, CC ECO:0000256|SAAS:SAAS00683545}. CC -!- PTM: Is synthesized initially as an inactive proenzyme, which is CC activated by self-cleavage at a specific serine bond to produce a CC beta-subunit with a hydroxyl group at its C-terminus and an alpha- CC subunit with a pyruvoyl group at its N-terminus. CC {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|PIRSR:PIRSR006246- CC 3}. CC -!- SIMILARITY: Belongs to the PanD family. {ECO:0000256|HAMAP- CC Rule:MF_00446, ECO:0000256|SAAS:SAAS00683551}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAO04394.1}. 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; BAZG01000129; GAO04394.1; -; Genomic_DNA. DR RefSeq; WP_011423097.1; NZ_BAZG01000129.1. DR SMR; A0A0D6QLW5; -. DR EnsemblBacteria; GAO04394; GAO04394; PSR1_03288. DR UniPathway; UPA00028; UER00002. DR Proteomes; UP000032665; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006523; P:alanine biosynthetic process; IEA:InterPro. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd06919; Asp_decarbox; 1. DR HAMAP; MF_00446; PanD; 1. DR InterPro; IPR009010; Asp_de-COase-like_dom_sf. DR InterPro; IPR003190; Asp_decarbox. DR PANTHER; PTHR21012; PTHR21012; 1. DR Pfam; PF02261; Asp_decarbox; 1. DR PIRSF; PIRSF006246; Asp_decarbox; 1. DR ProDom; PD009294; Asp_decarbox; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR TIGRFAMs; TIGR00223; panD; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_00446}; KW Complete proteome {ECO:0000313|Proteomes:UP000032665}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|SAAS:SAAS00683553}; KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|SAAS:SAAS00683555}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|SAAS:SAAS00683556}; KW Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|SAAS:SAAS00683542}; KW Pyruvate {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|PIRSR:PIRSR006246-1, ECO:0000256|SAAS:SAAS00683549}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|PIRSR:PIRSR006246-1, ECO:0000256|SAAS:SAAS00683539}; KW Zymogen {ECO:0000256|HAMAP-Rule:MF_00446}. FT CHAIN 1 24 Aspartate 1-decarboxylase. FT {ECO:0000256|PIRSR:PIRSR006246-5}. FT /FTId=PRO_5001427563. FT CHAIN 25 131 Aspartate 1-decarboxylase. FT {ECO:0000256|PIRSR:PIRSR006246-5}. FT /FTId=PRO_5001427562. FT REGION 73 75 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00446, ECO:0000256|PIRSR: FT PIRSR006246-2}. FT ACT_SITE 25 25 Schiff-base intermediate with substrate; FT via pyruvic acid. {ECO:0000256|HAMAP- FT Rule:MF_00446, ECO:0000256|PIRSR: FT PIRSR006246-1}. FT ACT_SITE 58 58 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00446, ECO:0000256|PIRSR:PIRSR006246- FT 1}. FT BINDING 57 57 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00446, ECO:0000256|PIRSR:PIRSR006246- FT 2}. FT MOD_RES 25 25 Pyruvic acid (Ser). {ECO:0000256|HAMAP- FT Rule:MF_00446, ECO:0000256|PIRSR: FT PIRSR006246-3}. SQ SEQUENCE 131 AA; 14517 MW; 8C2CFB1FDCDE5C38 CRC64; MRRTFFKAKI HRATVTHADL EYEGSVSIDE DLLEAAGIWE YEAVHVWNIT RGTRLQTYAI KGERGSGIIC INGAAAHLNR PGDMVILATF AELEEAEARD FKPTVVLVDR QNKIVAKDAV EVPGPARRVT A //