BCRA_THAAR
ID BCRA_THAAR Reviewed; 438 AA.
AC O87876;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Benzoyl-CoA reductase subunit A;
DE EC=1.3.7.8 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
DE AltName: Full=3-hydroxybenzoyl-CoA reductase subunit alpha;
DE EC=1.3.99.n1 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
GN Name=bcrA;
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 1-17, 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:8575453};
CC Note=The iron-sulfur cluster may be a [4Fe-4S] cluster.
CC {ECO:0000269|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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ224959; CAA12249.1; -; Genomic_DNA.
DR AlphaFoldDB; O87876; -.
DR SMR; O87876; -.
DR KEGG; ag:CAA12249; -.
DR BioCyc; MetaCyc:BCRATHAUERA-MON; -.
DR BRENDA; 1.3.7.8; 6271.
DR SABIO-RK; O87876; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR002731; ATPase_BadF.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR011954; Benzoyl_CoA_Rdtase_A.
DR InterPro; IPR008275; CoA_E_activase.
DR Pfam; PF01869; BcrAD_BadFG; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR02259; benz_CoA_red_A; 1.
DR TIGRFAMs; TIGR00241; CoA_E_activ; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Aromatic hydrocarbons catabolism; ATP-binding;
KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..438
FT /note="Benzoyl-CoA reductase subunit A"
FT /id="PRO_0000350730"
FT BINDING 298
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with BcrD"
FT /evidence="ECO:0000255"
FT BINDING 337
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with BcrD"
FT /evidence="ECO:0000255"
SQ SEQUENCE 438 AA; 48359 MW; 8F9E470FF688EAB7 CRC64;
MECFVGIDLG STTTKAVVMD DKGQVLGRGI TNSRSNYDTA ARVSKLEAFI DARLSLIRRE
LDKEPAVAGR VDEIIDGLTR NFRREQFIEQ LGDLEQTCVA NVEGPRFAGK EKAIVGALTE
VFRRLREEEA DKLFAPDAQR KSDFFRDLAG SRFMQIGEEV ARANGVEFDH LLHMYDKSII
EVENRPPSAD MNRKFRSAME RVRGEMSSAL DTAALGAPID AALEIDMSER YVVGTGYGRV
RLPFPKEHIR SEILCHGLGA HLMYPKTRTV LDIGGQDTKG IQIDDKGIVV NFQMNDRCAA
GTGRYLGYVA DEMNMGLHEL GPLAMKSTKS IRINSTCTVF AGAELRDRLA LGDKREDILA
GLHRAIMLRA MSIISRSGGI TDQFTFTGGV AKNEAAVKEL RQLVKENYGE VQINIDPDSI
YTGALGASEF ARRAVVEA
