HCRC_THAAR
ID HCRC_THAAR Reviewed; 161 AA.
AC O33818;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=4-hydroxybenzoyl-CoA reductase subunit gamma;
DE Short=4-HBCR subunit gamma;
DE EC=1.1.7.1 {ECO:0000269|PubMed:9490068};
GN Name=hcrC;
OS Thauera aromatica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=59405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=DSM 6984 / CIP 107765 / K172;
RX PubMed=9490068; DOI=10.1046/j.1432-1327.1998.2510916.x;
RA Breese K., Fuchs G.;
RT "4-hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying
RT bacterium Thauera aromatica -- prosthetic groups, electron donor, and genes
RT of a member of the molybdenum-flavin-iron-sulfur proteins.";
RL Eur. J. Biochem. 251:916-923(1998).
RN [2]
RP COFACTOR, EPR SPECTROSCOPY, AND MOSSBAUER SPECTROSCOPY.
RC STRAIN=DSM 6984 / CIP 107765 / K172;
RX PubMed=11602591; DOI=10.1074/jbc.m106766200;
RA Boll M., Fuchs G., Meier C., Trautwein A., El Kasmi A., Ragsdale S.W.,
RA Buchanan G., Lowe D.J.;
RT "Redox centers of 4-hydroxybenzoyl-CoA reductase, a member of the xanthine
RT oxidase family of molybdenum-containing enzymes.";
RL J. Biol. Chem. 276:47853-47862(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH 2 [2FE-2S] CLUSTERS
RP AND SUBUNIT ALPHA AND BETA, COFACTOR, AND SUBUNIT.
RX PubMed=15576037; DOI=10.1016/j.str.2004.10.008;
RA Unciuleac M., Warkentin E., Page C.C., Boll M., Ermler U.;
RT "Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase
RT with an additional [4Fe-4S] cluster and an inverted electron flow.";
RL Structure 12:2249-2256(2004).
CC -!- FUNCTION: Component of a complex that catalyzes the reductive
CC dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA. Reaction is not
CC reversible. Is a key enzyme in the anaerobic degradation of phenolic
CC compounds. {ECO:0000269|PubMed:9490068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + H2O + oxidized 2[4Fe-4S]-[ferredoxin] = 4-
CC hydroxybenzoyl-CoA + 2 H(+) + reduced 2[4Fe-4S]-[ferredoxin];
CC Xref=Rhea:RHEA:29603, Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33722,
CC ChEBI:CHEBI:33723, ChEBI:CHEBI:57356, ChEBI:CHEBI:57369; EC=1.1.7.1;
CC Evidence={ECO:0000269|PubMed:9490068};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:11602591, ECO:0000269|PubMed:15576037};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000269|PubMed:11602591, ECO:0000269|PubMed:15576037};
CC -!- ACTIVITY REGULATION: Inactivated by low concentrations of cyanide in
CC vitro. {ECO:0000269|PubMed:9490068}.
CC -!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
CC {ECO:0000269|PubMed:15576037, ECO:0000269|PubMed:9490068}.
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DR EMBL; AJ001830; CAA05037.1; -; Genomic_DNA.
DR PDB; 1RM6; X-ray; 1.60 A; C/F=1-161.
DR PDB; 1SB3; X-ray; 2.20 A; C/F=1-161.
DR PDBsum; 1RM6; -.
DR PDBsum; 1SB3; -.
DR AlphaFoldDB; O33818; -.
DR SMR; O33818; -.
DR DIP; DIP-48468N; -.
DR IntAct; O33818; 1.
DR KEGG; ag:CAA05037; -.
DR BioCyc; MetaCyc:COHBENREDTHAUERA-MON; -.
DR EvolutionaryTrace; O33818; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018525; F:4-hydroxybenzoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR017606; 4hydrxbenzoyl-CoA_Rdtase_gsu.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR03193; 4hydroxCoAred; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase.
FT CHAIN 1..161
FT /note="4-hydroxybenzoyl-CoA reductase subunit gamma"
FT /id="PRO_0000083927"
FT DOMAIN 3..79
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 41
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT BINDING 61
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT BINDING 100
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT BINDING 103
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT BINDING 135
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT BINDING 137
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:1RM6"
SQ SEQUENCE 161 AA; 17158 MW; CC2D8172F8EBA03B CRC64;
MKNILRLTLN GRAREDLVPD NMLLLDYLRE TVGLTGTKQG CDGGECGACT VLVDDRPRLA
CSTLAHQVAG KKVETVESLA TQGTLSKLQA AFHEKLGTQC GFCTPGMIMA SEALLRKNPS
PSRDEIKAAL AGNLCRCTGY VRSSKSVETA AAARLCEEGA R
