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-FEB-2023, entry version 47.
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.
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}.
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DR   EMBL; BAZG01000129; GAO04394.1; -; Genomic_DNA.
DR   RefSeq; WP_011423097.1; NZ_BAZG01000129.1.
DR   AlphaFoldDB; A0A0D6QLW5; -.
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   Gene3D; 2.40.40.20; -; 1.
DR   HAMAP; MF_00446; PanD; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003190; Asp_decarbox.
DR   PANTHER; PTHR21012; ASPARTATE 1-DECARBOXYLASE; 1.
DR   PANTHER; PTHR21012:SF0; ASPARTATE 1-DECARBOXYLASE; 1.
DR   Pfam; PF02261; Asp_decarbox; 1.
DR   PIRSF; PIRSF006246; Asp_decarbox; 1.
DR   SUPFAM; SSF50692; ADC-like; 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_5011837080"
FT   CHAIN           25..131
FT                   /note="Aspartate 1-decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00446,
FT                   ECO:0000256|PIRSR:PIRSR006246-5"
FT                   /id="PRO_5011837076"
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
//