HPDS_CLODI
ID HPDS_CLODI Reviewed; 85 AA.
AC Q84F15;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=4-hydroxyphenylacetate decarboxylase small subunit {ECO:0000303|PubMed:16878993};
DE Short=HPA decarboxylase small subunit;
DE EC=4.1.1.83 {ECO:0000269|PubMed:11231288, ECO:0000269|PubMed:16878993};
DE AltName: Full=4-hydroxyphenylacetate decarboxylase gamma subunit {ECO:0000250|UniProtKB:Q38HX3};
DE AltName: Full=p-hydroxyphenylacetate decarboxylase small subunit {ECO:0000303|PubMed:15153112};
GN Name=hpdC {ECO:0000312|EMBL:CAD65890.1};
OS Clostridioides difficile (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=1496;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=ATCC 9689 / DSM 1296 / BCRC 10642 / JCM 1296 / NCIMB 10666 / NCTC
RC 11209 / 90556-M6S {ECO:0000312|EMBL:CAD65890.1};
RX PubMed=15153112; DOI=10.1111/j.1432-1033.2004.04152.x;
RA Andrei P.I., Pierik A.J., Zauner S., Andrei-Selmer L.C., Selmer T.;
RT "Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate
RT decarboxylase. A small subunit, HpdC, is essential for catalytic
RT activity.";
RL Eur. J. Biochem. 271:2225-2230(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND REACTION MECHANISM.
RC STRAIN=ATCC 9689 / DSM 1296 / BCRC 10642 / JCM 1296 / NCIMB 10666 / NCTC
RC 11209 / 90556-M6S {ECO:0000269|PubMed:11231288};
RX PubMed=11231288; DOI=10.1046/j.1432-1327.2001.02001.x;
RA Selmer T., Andrei P.I.;
RT "p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel
RT glycyl radical enzyme catalysing the formation of p-cresol.";
RL Eur. J. Biochem. 268:1363-1372(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 9689 / DSM 1296 / BCRC 10642 / JCM 1296 / NCIMB 10666 / NCTC
RC 11209 / 90556-M6S {ECO:0000269|PubMed:16878993};
RX PubMed=16878993; DOI=10.1021/bi060840b;
RA Yu L., Blaser M., Andrei P.I., Pierik A.J., Selmer T.;
RT "4-Hydroxyphenylacetate decarboxylases: properties of a novel subclass of
RT glycyl radical enzyme systems.";
RL Biochemistry 45:9584-9592(2006).
CC -!- FUNCTION: Component of the HPA decarboxylase that decarboxylates
CC phenylacetates with a hydroxyl group in the p-position. Active toward
CC 4-hydroxyphenylacetate, 3,4-dihydroxyphenylacetate and to a lesser
CC extent p-hydroxymandelate (2-hydroxy-2-(4-hydroxyphenyl)acetate),
CC forming 4-methylphenol, 4-methylcatechol and 4-hydroxybenzylalcohol,
CC respectively. Is likely involved in the catabolism of aromatic amino
CC acids such as tyrosine fermentation. 4-methylphenol (p-cresol)
CC formation provides metabolic toxicity, which may benefit the pathogen
CC C.difficile by suppression of the endogenous gastrointestinal
CC microflora, allowing the development of gastrointestinal infections.
CC The small subunit is essential for enzymatic activity of HPA
CC decarboxylase, and seems also involved in the regulation of the enzyme
CC oligomeric state and catalytic activity. {ECO:0000269|PubMed:11231288,
CC ECO:0000269|PubMed:16878993}.
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:0000269|PubMed:11231288, ECO:0000269|PubMed:16878993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22733;
CC Evidence={ECO:0000305|PubMed:11231288, ECO:0000305|PubMed:16878993};
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:0000269|PubMed:11231288, ECO:0000269|PubMed:16878993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62557;
CC Evidence={ECO:0000305|PubMed:11231288, ECO:0000305|PubMed:16878993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-2-(4-hydroxyphenyl)acetate + H(+) = 4-hydroxybenzyl
CC alcohol + CO2; Xref=Rhea:RHEA:62588, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:32804, ChEBI:CHEBI:67410;
CC Evidence={ECO:0000269|PubMed:11231288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62589;
CC Evidence={ECO:0000305|PubMed:11231288};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:16878993};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:16878993};
CC -!- ACTIVITY REGULATION: Enzyme activity catalyzed by the HPA decarboxylase
CC complex is rapidly and irreversibly inactivated by oxygen.
CC Competitively inhibited by p-hydroxyphenylacetamide. Not inhibited by
CC m- or o-hydroxyphenyl-acetate, p-hydroxybenzoate or p-
CC hydroxyphenylpropionate. {ECO:0000269|PubMed:11231288}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:11231288};
CC Temperature dependence:
CC Has a half-life of 15 minutes at 30 degrees Celsius.
CC {ECO:0000269|PubMed:11231288};
CC -!- SUBUNIT: Heterooctamer consisting of 4 large (HpdB) subunits and 4
CC small (HpdC) subunits. {ECO:0000269|PubMed:15153112,
CC ECO:0000269|PubMed:16878993}.
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; AJ543426; CAD65890.1; -; Genomic_DNA.
DR RefSeq; WP_003425410.1; NZ_WBMC01000010.1.
DR AlphaFoldDB; Q84F15; -.
DR SMR; Q84F15; -.
DR GeneID; 66352701; -.
DR KEGG; ag:CAD65890; -.
DR BioCyc; MetaCyc:MON-18508; -.
DR BRENDA; 4.1.1.83; 1473.
DR SABIO-RK; Q84F15; -.
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 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding.
FT CHAIN 1..85
FT /note="4-hydroxyphenylacetate decarboxylase small subunit"
FT /id="PRO_0000403694"
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; 9504 MW; 1CB09CC84B155CD5 CRC64;
MRKHSDCMNF CAVDATKGIC RLSKQMINLD DAACPEIKVM PKCKNCKNFV EANDEGIGKC
VGLEKEDWVY STLNAITCEG HVFNE
