ID   A0A0D6QLW5_9DELT        Unreviewed;       131 AA.
AC   A0A0D6QLW5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   11-MAY-2016, entry version 11.
DE   RecName: Full=Aspartate 1-decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00575041};
DE            EC=4.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00575037};
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, 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-
RT   reducing bacterium, Anaeromyxobacter sp. strain PSR-1.";
RL   Appl. Environ. Microbiol. 79:4635-4642(2013).
RN   [2] {ECO:0000313|Proteomes:UP000032665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSR-1 {ECO:0000313|Proteomes:UP000032665};
RA   Tonomura M., Ehara A., Suzuki H., Amachi S.;
RT   "Draft Genome Sequence of Anaeromyxobacter sp. Strain PSR-1, an
RT   Arsenate-Respiring Bacterium Isolated from Arsenic-Contaminated
RT   Soil.";
RL   Genome Announc.3:e00472-15(2015).
CC   -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of
CC       aspartate to produce beta-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_00446, ECO:0000256|SAAS:SAAS00575033}.
CC   -!- CATALYTIC ACTIVITY: L-aspartate = beta-alanine + CO(2).
CC       {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00575035}.
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:SAAS00575028}.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00575044}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446,
CC       ECO:0000256|SAAS:SAAS00575020}.
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:SAAS00575047}.
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   RefSeq; WP_011423097.1; NZ_BAZG01000129.1.
DR   ProteinModelPortal; 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-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   Complete proteome {ECO:0000313|Proteomes:UP000032665};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00575014};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00575024};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00575019};
KW   Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00575029};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|PIRSR:PIRSR006246-1, ECO:0000256|SAAS:SAAS00575017};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|PIRSR:PIRSR006246-1, ECO:0000256|SAAS:SAAS00575048};
KW   Zymogen {ECO:0000256|HAMAP-Rule:MF_00446}.
FT   CHAIN         1     24       Aspartate 1-decarboxylase.
FT                                {ECO:0000256|PIRSR:PIRSR006246-5}.
FT                                /FTId=PRO_5001427563.
FT   CHAIN         1     24       Aspartate 1-decarboxylase.
FT                                {ECO:0000256|HAMAP-Rule:MF_00446}.
FT                                /FTId=PRO_5005017969.
FT   CHAIN        25    131       Aspartate 1-decarboxylase.
FT                                {ECO:0000256|PIRSR:PIRSR006246-5}.
FT                                /FTId=PRO_5001427562.
FT   CHAIN        25    131       Aspartate 1-decarboxylase.
FT                                {ECO:0000256|HAMAP-Rule:MF_00446}.
FT                                /FTId=PRO_5005017970.
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
//