BOXA_AROEV
ID BOXA_AROEV Reviewed; 414 AA.
AC Q9AIX6;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Benzoyl-CoA oxygenase component A;
DE EC=1.14.13.208 {ECO:0000269|PubMed:15458418};
DE AltName: Full=Benzoyl-CoA 2,3-dioxygenase subunit A;
DE AltName: Full=Benzoyl-CoA dioxygenase reductase component;
GN Name=boxA;
OS Aromatoleum evansii (Azoarcus evansii).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=59406;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19 AND 300-321,
RP COFACTOR, SUBUNIT, AND INDUCTION.
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX PubMed=11222587; DOI=10.1128/jb.183.6.1899-1908.2001;
RA Mohamed M.E.-S., Zaar A., Ebenau-Jehle C., Fuchs G.;
RT "Reinvestigation of a new type of aerobic benzoate metabolism in the
RT proteobacterium Azoarcus evansii.";
RL J. Bacteriol. 183:1899-1908(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX PubMed=12399500; DOI=10.1128/jb.184.22.6301-6315.2002;
RA Gescher J., Zaar A., Mohamed M.E.-S., Schaegger H., Fuchs G.;
RT "Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus
RT evansii.";
RL J. Bacteriol. 184:6301-6315(2002).
RN [3]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX PubMed=15458418; DOI=10.1111/j.1365-2958.2004.04263.x;
RA Zaar A., Gescher J., Eisenreich W., Bacher A., Fuchs G.;
RT "New enzymes involved in aerobic benzoate metabolism in Azoarcus evansii.";
RL Mol. Microbiol. 54:223-238(2004).
CC -!- FUNCTION: The BoxA/BoxB complex catalyzes the aerobic
CC reduction/oxygenation of the aromatic ring of benzoyl-CoA to form 2,3-
CC epoxy-2,3-dihydrobenzoyl-CoA. BoxA acts as a reductase that uses NADPH
CC to reduce the oxygenase component BoxB. BoxAB does not act on NADH or
CC benzoate. {ECO:0000269|PubMed:15458418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + H(+) + NADPH + O2 = 2,3-epoxy-2,3-
CC dihydrobenzoyl-CoA + H2O + NADP(+); Xref=Rhea:RHEA:48312,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57369, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:88118; EC=1.14.13.208;
CC Evidence={ECO:0000269|PubMed:15458418};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11222587};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11222587};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:11222587};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:11222587};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.03 mM for benzoyl-CoA {ECO:0000269|PubMed:15458418};
CC -!- SUBUNIT: Homodimer. The subunit composition of the active BoxA/BoxB
CC protein complex is not known. {ECO:0000269|PubMed:11222587}.
CC -!- INDUCTION: By benzoate. {ECO:0000269|PubMed:11222587}.
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DR EMBL; AF220510; AAK00600.1; -; Genomic_DNA.
DR EMBL; AF548005; AAN39377.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AIX6; -.
DR SMR; Q9AIX6; -.
DR KEGG; ag:AAN39377; -.
DR BioCyc; MetaCyc:MON-3142; -.
DR BRENDA; 1.14.13.208; 603.
DR SABIO-RK; Q9AIX6; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; 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 Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR017634; Benzoyl_CoA_Oase_BoxA.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR015701; FNR.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43314; PTHR43314; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00037; Fer4; 2.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF501177; BoxA; 1.
DR PIRSF; PIRSF000361; Frd-NADP+_RD; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR TIGRFAMs; TIGR03224; benzo_boxA; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Aromatic hydrocarbons catabolism; Dioxygenase;
KW Direct protein sequencing; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; NADP; Oxidoreductase; Repeat.
FT CHAIN 1..414
FT /note="Benzoyl-CoA oxygenase component A"
FT /id="PRO_0000350726"
FT DOMAIN 12..41
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 42..70
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 143..265
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 274..291
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 414 AA; 45883 MW; 1EDE1C61141DFFC7 CRC64;
MNAPAEHANL ARQHLIDPEI CIRCNTCEEI CPVDAITHDS RNYVVKFETC NGCLACISPC
PTGAIDSWRN VDKATPHSLA DQYSWDYLPD TTELDQFEAT VMGAAELPAE VQQITEVATA
GQGGPAMAPW SASHPYVNLY TPANPITATV TGNYRLTAED ASSDIHHIVL DFGTTPFPVL
EGQSIGIIPP GVDEKGKPHL LRMYSVASPR DGERPHYNNL SLTVKRVVED HEGNPTRGVA
SNYVCDLKKG DKVQVTGPYG STYLMPNHPG SSIMMICTGT GSAPMRAMTE RRRRRMDRKE
GGELVLFFGA RAPEELPYFG PLQKLPKEFI DINFAFSRVP GEPKRYVQDA IRERADKVFQ
MLQDDNCYIY ICGLKGMEAG VLEAFRDICR AKGADWDALR PQLLSKARFH VETY
