(data stored in ACNUC1104 zone)

SWISSPROT: PAND_NOCSJ

ID   PAND_NOCSJ              Reviewed;         139 AA.
AC   A1SDW8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Aspartate 1-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446};
DE            EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00446};
DE   AltName: Full=Aspartate alpha-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446};
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00446};
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00446};
DE   Flags: Precursor;
GN   Name=panD {ECO:0000255|HAMAP-Rule:MF_00446};
GN   OrderedLocusNames=Noca_0461;
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of
CC       aspartate to produce beta-alanine. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-aspartate = beta-alanine + CO2;
CC         Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00446};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00446};
CC       Note=Binds 1 pyruvoyl group covalently per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00446};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       beta-alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00446}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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
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:0000255|HAMAP-Rule:MF_00446}.
CC   -!- SIMILARITY: Belongs to the PanD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABL80003.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000509; ABL80003.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041546119.1; NC_008699.1.
DR   SMR; A1SDW8; -.
DR   STRING; 196162.Noca_0461; -.
DR   EnsemblBacteria; ABL80003; ABL80003; Noca_0461.
DR   KEGG; nca:Noca_0461; -.
DR   eggNOG; ENOG4108Z2X; Bacteria.
DR   eggNOG; COG0853; LUCA.
DR   HOGENOM; HOG000221007; -.
DR   KO; K01579; -.
DR   OrthoDB; 1751990at2; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000000640; Chromosome.
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   ProDom; PD009294; Asp_decarbox; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR00223; panD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SDW8.
DR   SWISS-2DPAGE; A1SDW8.
KW   Autocatalytic cleavage; Complete proteome; Cytoplasm; Decarboxylase;
KW   Lyase; Pantothenate biosynthesis; Pyruvate; Reference proteome;
KW   Schiff base; Zymogen.
FT   CHAIN         1     24       Aspartate 1-decarboxylase beta chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_00446}.
FT                                /FTId=PRO_0000307039.
FT   CHAIN        25    139       Aspartate 1-decarboxylase alpha chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_00446}.
FT                                /FTId=PRO_0000307040.
FT   REGION       73     75       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   ACT_SITE     25     25       Schiff-base intermediate with substrate;
FT                                via pyruvic acid. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   ACT_SITE     58     58       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   BINDING      57     57       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   MOD_RES      25     25       Pyruvic acid (Ser). {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
SQ   SEQUENCE   139 AA;  14643 MW;  53608BA31AD2A52C CRC64;
     MLRTMMKSKI HRATVTQADL HYVGSVTVDE DLLDAADLLP GELVHIVDID NGARLETYTI
     AGERGSGVIG INGAAARLVH PGDLVILIAY GQMEDVEAKG FEPHVVFVDA DNRVVSTGSD
     PADAPAGSGL LRGDRPAGR
//

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