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   16-JUN-2009, entry version 22.
DE   RecName: Full=Benzoyl-CoA reductase subunit C;
DE            EC=1.3.99.15;
DE   AltName: Full=3-hydroxybenzoyl-CoA reductase subunit gamma;
DE            EC=1.3.99.n1;
GN   Name=bcrC;
OS   Thauera aromatica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Thauera.
OX   NCBI_TaxID=59405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18; 119-130
RP   AND 218-229, AND SUBUNIT.
RC   STRAIN=DSM 6984 / K172;
RX   MEDLINE=98417440; PubMed=9746358;
RX   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
RT   metabolism in the bacterium Thauera aromatica.";
RL   Eur. J. Biochem. 256:148-154(1998).
RN   [2]
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND COFACTOR.
RC   STRAIN=DSM 6984 / 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
RT   anaerobic aromatic metabolism. ATP dependence of the reaction,
RT   purification and some properties of the enzyme from Thauera aromatica
RT   strain K172.";
RL   Eur. J. Biochem. 234:921-933(1995).
RN   [3]
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=DSM 6984 / K172;
RX   MEDLINE=21142524; 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
RT   bacterium 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
CC       3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The
CC       enzyme also reduces other benzoyl-CoA analogs with small
CC       substituents at the aromatic ring.
CC   -!- CATALYTIC ACTIVITY: Benzoyl-CoA + reduced acceptor + 2 ATP =
CC       cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: 3-hydroxybenzoyl-CoA + reduced acceptor + 2
CC       ATP = 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2
CC       ADP + 2 phosphate.
CC   -!- COFACTOR: Iron-sulfur.
CC   -!- COFACTOR: Flavin (Probable).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=15 uM for benzoyl-CoA;
CC         KM=20 uM for 3-hydroxybenzoyl-CoA;
CC         KM=600 uM for ATP;
CC       pH dependence:
CC         Optimum pH is 7.2-7.5;
CC   -!- SUBUNIT: Heterotetramer composed of A, B, C, and D subunits.
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DR   EMBL; AJ224959; CAA12247.1; -; Genomic_DNA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0018522; F:benzoyl-CoA reductase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR011958; Benzoyl_CoA_Rdtase_C.
DR   InterPro; IPR010327; HGD-D.
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;
KW   Direct protein sequencing; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotide-binding; Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    386       Benzoyl-CoA reductase subunit C.
FT                                /FTId=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
//