HPDS_CLOSL
ID HPDS_CLOSL Reviewed; 86 AA.
AC Q38HX3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=4-hydroxyphenylacetate decarboxylase small subunit {ECO:0000305|PubMed:16878993};
DE Short=HPA decarboxylase small subunit;
DE EC=4.1.1.83 {ECO:0000269|PubMed:16878993};
DE AltName: Full=4-hydroxyphenylacetate decarboxylase gamma subunit {ECO:0000303|PubMed:21823587};
DE AltName: Full=p-hydroxyphenylacetate decarboxylase small subunit {ECO:0000305|PubMed:16878993};
GN Name=csdC {ECO:0000312|EMBL:ABB05047.1};
OS Clostridium scatologenes.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 25775 / DSM 757 / JCM 1414 / NCIB 8855 / VPI 5393
RC {ECO:0000312|EMBL:ABB05047.1};
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).
RN [2] {ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH HPA DECARBOXYLASE
RP LARGE SUBUNIT AND IRON-SULFUR (4FE-4S) CLUSTERS, COFACTOR, SUBUNIT, AND
RP REACTION MECHANISM.
RX PubMed=21823587; DOI=10.1021/ja203344x;
RA Martins B.M., Blaser M., Feliks M., Ullmann G.M., Buckel W., Selmer T.;
RT "Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl
RT radical enzyme.";
RL J. Am. Chem. Soc. 133:14666-14674(2011).
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
CC (PubMed:16878993). The small subunit is essential for enzymatic
CC activity of HPA decarboxylase, and seems also involved in the
CC regulation of the enzyme oligomeric state and catalytic activity (By
CC similarity). {ECO:0000250|UniProtKB:Q84F15,
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:16878993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22733;
CC Evidence={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:16878993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62557;
CC Evidence={ECO:0000305|PubMed:16878993};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:16878993, ECO:0000269|PubMed:21823587};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:16878993, ECO:0000269|PubMed:21823587};
CC -!- SUBUNIT: Heterooctamer consisting of 4 large (HpdB) subunits and 4
CC small (HpdC) subunits, arranged as a tetramer of heterodimers.
CC {ECO:0000269|PubMed:16878993, ECO:0000269|PubMed:21823587}.
CC -!- SIMILARITY: Belongs to the HPA decarboxylase small subunit family.
CC {ECO:0000305}.
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DR EMBL; DQ227741; ABB05047.1; -; Genomic_DNA.
DR RefSeq; WP_029163540.1; NZ_CP009933.1.
DR PDB; 2Y8N; X-ray; 1.75 A; B/D=1-86.
DR PDB; 2YAJ; X-ray; 1.81 A; B/D=1-86.
DR PDBsum; 2Y8N; -.
DR PDBsum; 2YAJ; -.
DR AlphaFoldDB; Q38HX3; -.
DR SMR; Q38HX3; -.
DR STRING; 1548.CSCA_5036; -.
DR OrthoDB; 1917552at2; -.
DR SABIO-RK; Q38HX3; -.
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 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding.
FT CHAIN 1..86
FT /note="4-hydroxyphenylacetate decarboxylase small subunit"
FT /id="PRO_0000403696"
FT BINDING 3
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ"
FT BINDING 6
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ"
FT BINDING 36
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ"
FT BINDING 80
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2Y8N"
SQ SEQUENCE 86 AA; 9343 MW; 29A7B3C5B66AAB6D CRC64;
MRHYDCKNYI NLDCEKGLCA LTKGMVPIDG EGSEACPNFK PAEKCGNCKN FCNPDKYGLG
TCTGLEKENW AYATCGASAC PSYKAE
