ID A0A365PS37_9PSED Unreviewed; 126 AA. AC A0A365PS37; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 03-JUL-2019, entry version 6. 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 beta chain {ECO:0000256|HAMAP-Rule:MF_00446}; DE Contains: DE RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00446}; GN Name=panD {ECO:0000256|HAMAP-Rule:MF_00446}; GN ORFNames=DQ403_15415 {ECO:0000313|EMBL:RBA55686.1}; OS Pseudomonas zhaodongensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1176257 {ECO:0000313|EMBL:RBA55686.1, ECO:0000313|Proteomes:UP000252554}; RN [1] {ECO:0000313|EMBL:RBA55686.1, ECO:0000313|Proteomes:UP000252554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SST2 {ECO:0000313|EMBL:RBA55686.1, RC ECO:0000313|Proteomes:UP000252554}; RA Abdel-Mageed W.M., Lehri B., Jarmusch S.A., Miranda K., Goodfellow M., RA Jaspars M., Karlyshev A.V.; RT "Whole genome sequencing of four bacterial strains from South Shetland RT trench revealing bio-synthetic gene clusters."; RL Submitted (JUN-2018) 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: CC Reaction=H(+) + L-aspartate = beta-alanine + CO2; CC Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00446, CC ECO:0000256|SAAS:SAAS01125291}; 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: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, ECO:0000256|PIRSR:PIRSR006246- CC 3}. CC -!- SIMILARITY: Belongs to the PanD family. {ECO:0000256|HAMAP- CC Rule:MF_00446, ECO:0000256|SAAS:SAAS01091904}. 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:RBA55686.1}. 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; QNTV01000012; RBA55686.1; -; Genomic_DNA. DR RefSeq; WP_019342093.1; NZ_QNTV01000012.1. DR UniPathway; UPA00028; UER00002. DR Proteomes; UP000252554; 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 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:UP000252554}; 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, ECO:0000256|SAAS:SAAS00097768, KW ECO:0000313|EMBL:RBA55686.1}; 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, ECO:0000256|SAAS:SAAS00097789}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00446, KW ECO:0000256|PIRSR:PIRSR006246-1, ECO:0000256|SAAS:SAAS00097793}; KW Zymogen {ECO:0000256|HAMAP-Rule:MF_00446}. FT CHAIN 1 24 Aspartate 1-decarboxylase beta chain. FT {ECO:0000256|PIRSR:PIRSR006246-5}. FT /FTId=PRO_5017108975. FT CHAIN 25 126 Aspartate 1-decarboxylase alpha chain. FT {ECO:0000256|PIRSR:PIRSR006246-5}. FT /FTId=PRO_5017108977. 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 126 AA; 13741 MW; 28797F21111E2115 CRC64; MHAIMLKAKL HRAQVTHSVL DYEGSCAIDG DWLDLAGIRE YEQIQIYNVD NGERFTTYAI RGEEGSKIIS VNGAAAHKAG VGHRVIICAY AHYSEAELAS FKPHVLYMGA DGDLSHTSNA IPVQVA //