ID A0A0D6QLW5_9DELT Unreviewed; 131 AA. AC A0A0D6QLW5; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 14-OCT-2015, entry version 5. DE RecName: Full=Aspartate 1-decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00097809}; DE EC=4.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00097718}; DE AltName: Full=Aspartate 1-decarboxylase; DE AltName: Full=Aspartate alpha-decarboxylase {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}; RN [1] {ECO:0000313|EMBL:GAO04394.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PSR-1 {ECO:0000313|EMBL:GAO04394.1}; 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|EMBL:GAO04394.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PSR-1 {ECO:0000313|EMBL:GAO04394.1}; RA Suzuki H., Tonomura M., Ehara A., Amachi S.; RT "Draft genome sequence of Anaeromyxobacter sp. PSR-1."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of CC aspartate to produce beta-alanine. {ECO:0000256|HAMAP- CC Rule:MF_00446, ECO:0000256|SAAS:SAAS00097795}. CC -!- CATALYTIC ACTIVITY: L-aspartate = beta-alanine + CO(2). CC {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00097780}. CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00446, CC ECO:0000256|SAAS:SAAS00179599}; CC Note=Binds 1 pyruvoyl group covalently per subunit. CC {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00179599}; CC -!- COFACTOR: CC Name=pyruvoyl group; Xref=ChEBI:CHEBI:45360; 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:SAAS00097721}. CC -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits. CC {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00097784}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446, CC ECO:0000256|SAAS:SAAS00097746}. 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}. CC -!- SIMILARITY: Belongs to the PanD family. {ECO:0000256|HAMAP- CC Rule:MF_00446}. 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 UniPathway; UPA00028; UER00002. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006523; P:alanine biosynthetic process; IEA:InterPro. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00446; PanD; 1. DR InterPro; IPR009010; Asp_de-COase-like_dom. 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|SAAS:SAAS00097775}; KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|SAAS:SAAS00097760}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|SAAS:SAAS00097768}; KW Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|SAAS:SAAS00097818}; KW Pyruvate {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|PIRSR:PIRSR006246-1}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|PIRSR:PIRSR006246-1}; 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 1 24 Aspartate 1-decarboxylase. FT {ECO:0000256|HAMAP-Rule:MF_00446}. FT /FTId=PRO_5005017969. FT CHAIN 25 131 Aspartate 1-decarboxylase. FT {ECO:0000256|PIRSR:PIRSR006246-5}. FT /FTId=PRO_5001427562. FT CHAIN 25 131 Aspartate 1-decarboxylase. FT {ECO:0000256|HAMAP-Rule:MF_00446}. FT /FTId=PRO_5005017970. 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}. 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 //