位置:首页 > 蛋白库 > HPDS_CLODR
HPDS_CLODR
ID   HPDS_CLODR              Reviewed;          85 AA.
AC   C9YHW2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=4-hydroxyphenylacetate decarboxylase small subunit {ECO:0000250|UniProtKB:Q38HX3};
DE            Short=HPA decarboxylase small subunit {ECO:0000250|UniProtKB:Q38HX3};
DE            EC=4.1.1.83 {ECO:0000250|UniProtKB:Q38HX3};
DE   AltName: Full=4-hydroxyphenylacetate decarboxylase gamma subunit {ECO:0000250|UniProtKB:Q38HX3};
DE   AltName: Full=p-hydroxyphenylacetate decarboxylase small subunit {ECO:0000250|UniProtKB:Q38HX3};
GN   Name=hpdC {ECO:0000312|EMBL:CBE01728.1}; OrderedLocusNames=CDR20291_0153;
OS   Clostridioides difficile (strain R20291) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=645463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R20291;
RX   PubMed=19781061; DOI=10.1186/gb-2009-10-9-r102;
RA   Stabler R.A., He M., Dawson L., Martin M., Valiente E., Corton C.,
RA   Lawley T.D., Sebaihia M., Quail M.A., Rose G., Gerding D.N., Gibert M.,
RA   Popoff M.R., Parkhill J., Dougan G., Wren B.W.;
RT   "Comparative genome and phenotypic analysis of Clostridium difficile 027
RT   strains provides insight into the evolution of a hypervirulent bacterium.";
RL   Genome Biol. 10:R102.1-R102.15(2009).
CC   -!- FUNCTION: Component of the HPA decarboxylase that decarboxylates
CC       phenylacetates with a hydroxyl group in the p-position. Active toward
CC       4-hydroxyphenylacetate and 3,4-dihydroxyphenylacetate, forming 4-
CC       methylphenol and 4-methylcatechol, respectively. Is likely involved in
CC       the catabolism of aromatic amino acids such as tyrosine fermentation.
CC       4-methylphenol (p-cresol) formation provides metabolic toxicity, which
CC       allows an active suppression of other microbes and may provide growth
CC       advantages for the producers in highly competitive environments (By
CC       similarity). The small subunit is essential for enzymatic activity of
CC       HPA decarboxylase, and seems also involved in the regulation of the
CC       enzyme oligomeric state and catalytic activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q38HX3, ECO:0000250|UniProtKB:Q84F15}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxyphenylacetate + H(+) = 4-methylphenol + CO2;
CC         Xref=Rhea:RHEA:22732, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17847, ChEBI:CHEBI:48999; EC=4.1.1.83;
CC         Evidence={ECO:0000250|UniProtKB:Q38HX3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22733;
CC         Evidence={ECO:0000250|UniProtKB:Q38HX3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,4-dihydroxyphenylacetate + H(+) = 4-methylcatechol + CO2;
CC         Xref=Rhea:RHEA:62556, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17254, ChEBI:CHEBI:17612; EC=4.1.1.83;
CC         Evidence={ECO:0000250|UniProtKB:Q38HX3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62557;
CC         Evidence={ECO:0000250|UniProtKB:Q38HX3};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q38HX3};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit.
CC       {ECO:0000250|UniProtKB:Q38HX3};
CC   -!- SUBUNIT: Heterooctamer consisting of 4 large (HpdB) subunits and 4
CC       small (HpdC) subunits, arranged as a tetramer of heterodimers.
CC       {ECO:0000250|UniProtKB:Q38HX3}.
CC   -!- SIMILARITY: Belongs to the HPA decarboxylase small subunit family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FN545816; CBE01728.1; -; Genomic_DNA.
DR   RefSeq; WP_009888000.1; NC_013316.1.
DR   AlphaFoldDB; C9YHW2; -.
DR   SMR; C9YHW2; -.
DR   EnsemblBacteria; CBE01728; CBE01728; CDR20291_0153.
DR   KEGG; cdl:CDR20291_0153; -.
DR   HOGENOM; CLU_187388_0_0_9; -.
DR   OMA; ANDEGIG; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043722; F:4-hydroxyphenylacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR041125; 4HPAD_g_N.
DR   InterPro; IPR040923; HpdC_C.
DR   Pfam; PF18671; 4HPAD_g_N; 1.
DR   Pfam; PF18524; HPIP_like; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding.
FT   CHAIN           1..85
FT                   /note="4-hydroxyphenylacetate decarboxylase small subunit"
FT                   /id="PRO_0000403695"
FT   BINDING         4
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX3"
FT   BINDING         7
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX3"
FT   BINDING         20
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX3"
FT   BINDING         34
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX3"
FT   BINDING         43
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX3"
FT   BINDING         46
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX3"
FT   BINDING         60
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX3"
FT   BINDING         78
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q38HX3"
SQ   SEQUENCE   85 AA;  9520 MW;  0EA29CC84B0ABCD5 CRC64;
     MRKHSDCMNF CAVDATKGIC RLSKQMINLD DSACPEIKVM PKCKNCKNFV EANDEGIGKC
     VGLEKEDWVY STLNAITCEG HVFNE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024