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-JUL-2015, entry version 3.
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         Evidence={ECO:0000256|PIRSR:PIRSR006246-1};
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}.
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}.
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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 beta chain.
FT                                {ECO:0000256|PIRSR:PIRSR006246-5}.
FT                                /FTId=PRO_5001421932.
FT   CHAIN        25    131       Aspartate 1-decarboxylase alpha chain.
FT                                {ECO:0000256|PIRSR:PIRSR006246-5}.
FT                                /FTId=PRO_5001421933.
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   131 AA;  14517 MW;  8C2CFB1FDCDE5C38 CRC64;
     MRRTFFKAKI HRATVTHADL EYEGSVSIDE DLLEAAGIWE YEAVHVWNIT RGTRLQTYAI
     KGERGSGIIC INGAAAHLNR PGDMVILATF AELEEAEARD FKPTVVLVDR QNKIVAKDAV
     EVPGPARRVT A
//