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PAND_RHOBA
ID   PAND_RHOBA              Reviewed;         156 AA.
AC   Q7UQU4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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}; OrderedLocusNames=RB6090;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC   -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate
CC       to produce beta-alanine. {ECO:0000255|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:0000255|HAMAP-
CC         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. {ECO:0000255|HAMAP-
CC       Rule:MF_00446};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-
CC       alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP-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 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:0000255|HAMAP-
CC       Rule:MF_00446}.
CC   -!- SIMILARITY: Belongs to the PanD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
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DR   EMBL; BX294143; CAD74603.1; -; Genomic_DNA.
DR   RefSeq; NP_867058.1; NC_005027.1.
DR   AlphaFoldDB; Q7UQU4; -.
DR   SMR; Q7UQU4; -.
DR   STRING; 243090.RB6090; -.
DR   EnsemblBacteria; CAD74603; CAD74603; RB6090.
DR   KEGG; rba:RB6090; -.
DR   PATRIC; fig|243090.15.peg.2934; -.
DR   eggNOG; COG0853; Bacteria.
DR   HOGENOM; CLU_115305_0_0_0; -.
DR   InParanoid; Q7UQU4; -.
DR   OMA; HEPKLVF; -.
DR   OrthoDB; 1751990at2; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004068; F:aspartate 1-decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0006523; P:alanine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IBA:GO_Central.
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   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR00223; panD; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Cytoplasm; Decarboxylase; Lyase;
KW   Pantothenate biosynthesis; Pyruvate; Reference proteome; Schiff base;
KW   Zymogen.
FT   CHAIN           1..28
FT                   /note="Aspartate 1-decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT                   /id="PRO_0000023147"
FT   CHAIN           29..156
FT                   /note="Aspartate 1-decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT                   /id="PRO_0000023148"
FT   ACT_SITE        29
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT   ACT_SITE        62
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT   BINDING         77..79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT   MOD_RES         29
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
SQ   SEQUENCE   156 AA;  16828 MW;  ABA3EBEC529C20C0 CRC64;
     MVDTPYRKML AAKIHRATVT GADVNYEGSL TVPPELLVAA KIHPYESLHV WNVTRGTRLE
     TYAIEGLPNS NDVCANGAAA HLIRPGDHVI LAAYAMVPEA DAATHKPRLI FVDDNNQLSH
     VGPEIAGPNL RSDSDDTHLV RSTEMTPDGQ PLAEGC
 
 
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