ID A0A0D6QLW5_9DELT Unreviewed; 131 AA. AC A0A0D6QLW5; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 12-OCT-2022, entry version 45. 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 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; OC unclassified 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-reducing RT bacterium, Anaeromyxobacter sp. strain PSR-1."; RL Appl. Environ. Microbiol. 79:4635-4642(2013). RN [2] {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}; RA Tonomura M., Ehara A., Suzuki H., Amachi S.; RT "Draft Genome Sequence of Anaeromyxobacter sp. Strain PSR-1, an Arsenate- RT Respiring Bacterium Isolated from Arsenic-Contaminated Soil."; RL Genome Announc. 3:e00472-15(2015). 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: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 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 /id="PRO_5011837080" FT CHAIN 1..24 FT /note="Aspartate 1-decarboxylase beta chain" FT /evidence="ECO:0000256|PIRSR:PIRSR006246-5" FT /id="PRO_5035516479" FT CHAIN 25..131 FT /note="Aspartate 1-decarboxylase alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00446" FT /id="PRO_5011837076" FT CHAIN 25..131 FT /note="Aspartate 1-decarboxylase alpha chain" FT /evidence="ECO:0000256|PIRSR:PIRSR006246-5" FT /id="PRO_5035516480" 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 BINDING 73..75 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 131 AA; 14517 MW; 8C2CFB1FDCDE5C38 CRC64; MRRTFFKAKI HRATVTHADL EYEGSVSIDE DLLEAAGIWE YEAVHVWNIT RGTRLQTYAI KGERGSGIIC INGAAAHLNR PGDMVILATF AELEEAEARD FKPTVVLVDR QNKIVAKDAV EVPGPARRVT A //