ID A0A6B3LI67_9BACT Unreviewed; 115 AA. AC A0A6B3LI67; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 03-AUG-2022, 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=GXP69_01265 {ECO:0000313|EMBL:NEM96309.1}; OS Pontibacter burrus. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Pontibacter. OX NCBI_TaxID=2704466 {ECO:0000313|EMBL:NEM96309.1, ECO:0000313|Proteomes:UP000474777}; RN [1] {ECO:0000313|EMBL:NEM96309.1, ECO:0000313|Proteomes:UP000474777} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BT327 {ECO:0000313|EMBL:NEM96309.1, RC ECO:0000313|Proteomes:UP000474777}; RA Kim M.K.; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate CC to produce beta-alanine. {ECO:0000256|HAMAP-Rule:MF_00446}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00446}; 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. {ECO:0000256|HAMAP- CC Rule:MF_00446, ECO:0000256|PIRSR:PIRSR006246-1}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta- CC alanine from L-aspartate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00446}. CC -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits. CC {ECO:0000256|HAMAP-Rule:MF_00446}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446}. CC -!- PTM: Is synthesized initially as an inactive proenzyme, which is CC activated by self-cleavage at a specific serine bond to produce a beta- CC subunit with a hydroxyl group at its C-terminus and an alpha-subunit CC with a pyruvoyl group at its N-terminus. {ECO:0000256|HAMAP- CC Rule:MF_00446, ECO:0000256|PIRSR:PIRSR006246-3}. CC -!- SIMILARITY: Belongs to the PanD family. {ECO:0000256|HAMAP- CC Rule:MF_00446}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NEM96309.1}. 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; JAAGWD010000001; NEM96309.1; -; Genomic_DNA. DR UniPathway; UPA00028; UER00002. DR Proteomes; UP000474777; 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|ARBA:ARBA00022813, ECO:0000256|HAMAP- KW Rule:MF_00446}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00446}; KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP- KW Rule:MF_00446}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00446}; KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655, KW ECO:0000256|HAMAP-Rule:MF_00446}; KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00446}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP- KW Rule:MF_00446}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00446}. FT CHAIN 1..24 FT /note="Aspartate 1-decarboxylase beta chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00446, FT ECO:0000256|PIRSR:PIRSR006246-5" FT /id="PRO_5025741403" FT CHAIN 25..115 FT /note="Aspartate 1-decarboxylase alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00446, FT ECO:0000256|PIRSR:PIRSR006246-5" FT /id="PRO_5025741404" FT REGION 73..75 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00446, FT ECO:0000256|PIRSR:PIRSR006246-2" FT ACT_SITE 25 FT /note="Schiff-base intermediate with substrate; via pyruvic FT acid" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00446, FT ECO:0000256|PIRSR:PIRSR006246-1" FT ACT_SITE 58 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00446, FT ECO:0000256|PIRSR:PIRSR006246-1" FT BINDING 57 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00446, FT ECO:0000256|PIRSR:PIRSR006246-2" FT MOD_RES 25 FT /note="Pyruvic acid (Ser)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00446, FT ECO:0000256|PIRSR:PIRSR006246-3" SQ SEQUENCE 115 AA; 12783 MW; 49F397DD5749707B CRC64; MYIEVLKSKI HRCKVTQAEL HYVGSITIDE DLMDAANVVE NEKVTIVNIN NGERFETYVI KGERGTGTVC LNGPAARKVQ VGDIVIVISY CSIPFAEAKA HKPTLVFPDQ HNRLV //