BCRC_THAAR
ID BCRC_THAAR Reviewed; 386 AA.
AC O87874;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Benzoyl-CoA reductase subunit C;
DE EC=1.3.7.8 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
DE AltName: Full=3-hydroxybenzoyl-CoA reductase subunit gamma;
DE EC=1.3.99.n1 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
GN Name=bcrC;
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 2-18; 119-130 AND
RP 218-229, AND SUBUNIT.
RC STRAIN=DSM 6984 / CIP 107765 / K172;
RX PubMed=9746358; DOI=10.1046/j.1432-1327.1998.2560148.x;
RA Breese K., Boll M., Alt-Moerbe J., Schaegger H., Fuchs G.;
RT "Genes coding for the benzoyl-CoA pathway of anaerobic aromatic metabolism
RT in the bacterium Thauera aromatica.";
RL Eur. J. Biochem. 256:148-154(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND COFACTOR.
RC STRAIN=DSM 6984 / CIP 107765 / K172;
RX PubMed=8575453; DOI=10.1111/j.1432-1033.1995.921_a.x;
RA Boll M., Fuchs G.;
RT "Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic
RT aromatic metabolism. ATP dependence of the reaction, purification and some
RT properties of the enzyme from Thauera aromatica strain K172.";
RL Eur. J. Biochem. 234:921-933(1995).
RN [3]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 6984 / CIP 107765 / K172;
RX PubMed=11208796; DOI=10.1128/jb.183.3.968-979.2001;
RA Laempe D., Jahn M., Breese K., Schaegger H., Fuchs G.;
RT "Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying bacterium
RT Thauera aromatica.";
RL J. Bacteriol. 183:968-979(2001).
CC -!- FUNCTION: Catalyzes the anaerobic reduction of benzoyl-CoA and 3-
CC hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-
CC hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme
CC also reduces other benzoyl-CoA analogs with small substituents at the
CC aromatic ring. {ECO:0000269|PubMed:8575453}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ADP + cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized 2[4Fe-
CC 4S]-[ferredoxin] + 2 phosphate = 2 ATP + benzoyl-CoA + 2 H2O +
CC reduced 2[4Fe-4S]-[ferredoxin]; Xref=Rhea:RHEA:30199, Rhea:RHEA-
CC COMP:10002, Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57369, ChEBI:CHEBI:57374,
CC ChEBI:CHEBI:456216; EC=1.3.7.8;
CC Evidence={ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybenzoyl-CoA + AH2 + 2 ATP + 2 H2O = 3-
CC hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + A + 2 ADP + 2 H(+) + 2
CC phosphate; Xref=Rhea:RHEA:25420, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57342,
CC ChEBI:CHEBI:58801, ChEBI:CHEBI:456216; EC=1.3.99.n1;
CC Evidence={ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
CC -!- COFACTOR:
CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC Evidence={ECO:0000269|PubMed:8575453};
CC -!- COFACTOR:
CC Name=an oxidized flavin; Xref=ChEBI:CHEBI:60531;
CC Evidence={ECO:0000305|PubMed:8575453};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for benzoyl-CoA {ECO:0000269|PubMed:11208796,
CC ECO:0000269|PubMed:8575453};
CC KM=20 uM for 3-hydroxybenzoyl-CoA {ECO:0000269|PubMed:11208796,
CC ECO:0000269|PubMed:8575453};
CC KM=600 uM for ATP {ECO:0000269|PubMed:11208796,
CC ECO:0000269|PubMed:8575453};
CC pH dependence:
CC Optimum pH is 7.2-7.5. {ECO:0000269|PubMed:11208796,
CC ECO:0000269|PubMed:8575453};
CC -!- SUBUNIT: Heterotetramer composed of A, B, C, and D subunits.
CC {ECO:0000269|PubMed:9746358}.
CC -!- SIMILARITY: Belongs to the FldB/FldC dehydratase alpha/beta subunit
CC family. {ECO:0000305}.
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DR EMBL; AJ224959; CAA12247.1; -; Genomic_DNA.
DR AlphaFoldDB; O87874; -.
DR SMR; O87874; -.
DR KEGG; ag:CAA12247; -.
DR BioCyc; MetaCyc:BCRCTHAUER-MON; -.
DR SABIO-RK; O87874; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0018522; F:benzoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR011958; Benzoyl_CoA_Rdtase_C.
DR InterPro; IPR010327; FldB/FldC_alpha/beta.
DR Pfam; PF06050; HGD-D; 1.
DR TIGRFAMs; TIGR02263; benz_CoA_red_C; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; ATP-binding; Direct protein sequencing;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Nucleotide-binding;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9746358"
FT CHAIN 2..386
FT /note="Benzoyl-CoA reductase subunit C"
FT /id="PRO_0000350732"
SQ SEQUENCE 386 AA; 43720 MW; 989BC3528A45EC6E CRC64;
MSTADIIARC EALYEDLDFT AARQWKEADP SRKVIAYMPV YVPREIIHAA GMLPLGIMGG
GDGLEVIHGD AFYQSYICRI PRSTIELGLS KRMDFVDGML FPSICDVIRN LSGMWKLMFP
GKYVRYFDVP QNYRDDVGGN YYTAELNELR EGLEHLSGRK ITDDALRASI KVYNENRKLV
QDVYGLRSRE PWKVPSADVY LLMRAGLVLP VEEHNQMLKD YLAAAVKVEA QKRDNCRVII
NGSFCEQPPL NLIKSIELSG CYIVDDDYMI VHRFLRNEVS TAGDPMQNLS LAFLHESIST
AAKYDDKEED KGKYLLEQVR TNAAEGVIFA APSFCDPALL ERPMLADRCS ENKVPYISFK
YAENSGQMQP IREQAGTFAD SIKLWS
