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}.
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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
