HCRB_THAAR
ID HCRB_THAAR Reviewed; 324 AA.
AC O33820;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=4-hydroxybenzoyl-CoA reductase subunit beta;
DE Short=4-HBCR subunit beta;
DE EC=1.1.7.1 {ECO:0000269|PubMed:9490068};
GN Name=hcrB;
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 1-30 AND 169-185,
RP FUNCTION, 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 FAD; [4FE-4S] CLUSTER
RP AND SUBUNIT ALPHA AND GAMMA, 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=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
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; CAA05039.1; -; Genomic_DNA.
DR PDB; 1RM6; X-ray; 1.60 A; B/E=1-324.
DR PDB; 1SB3; X-ray; 2.20 A; B/E=1-324.
DR PDBsum; 1RM6; -.
DR PDBsum; 1SB3; -.
DR AlphaFoldDB; O33820; -.
DR SMR; O33820; -.
DR DIP; DIP-48467N; -.
DR IntAct; O33820; 1.
DR KEGG; ag:CAA05039; -.
DR BioCyc; MetaCyc:BOHBENREDTHAUERA-MON; -.
DR EvolutionaryTrace; O33820; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018525; F:4-hydroxybenzoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 2.
DR InterPro; IPR017608; 4hydrxbenzoyl-CoA_Rdtase_bsu.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR03195; 4hydrxCoA_B; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase.
FT CHAIN 1..324
FT /note="4-hydroxybenzoyl-CoA reductase subunit beta"
FT /id="PRO_0000083926"
FT DOMAIN 2..217
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 29..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15576037"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15576037"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15576037"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15576037"
FT BINDING 122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 146
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15576037"
FT BINDING 224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15576037"
FT CONFLICT 22..30
FT /note="LAAEATLPL -> GTVPVAQLF (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:1SB3"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 235..245
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 248..262
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 302..322
FT /evidence="ECO:0007829|PDB:1RM6"
SQ SEQUENCE 324 AA; 34374 MW; C3C5ECAAD093F9DB CRC64;
MNILTDFRTH RPATLADAVN ALAAEATLPL GAGTDLLPNL RRGLGHPAAL VDLTGIDGLA
TISTLADGSL RIGAGATLEA IAEHDAIRTT WPALAQAAES VAGPTHRAAA TLGGNLCQDT
RCTFYNQSEW WRSGNGYCLK YKGDKCHVIV KSDRCYATYH GDVAPALMVL DARAEIVGPA
GKRTVPVAQL FRESGAEHLT LEKGELLAAI EVPPTGAWSA AYSKVRIRDA VDFPLAGVAA
ALQRDGDRIA GLRVAITGSN SAPLMVPVDA LLGGNWDDAA AETLAQLVRK TSNVLRTTIT
GVKYRRRVLL AISRKVVDQL WEAR
