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Database: UniProt
Entry: Q9AIX6
LinkDB: Q9AIX6
Original site: Q9AIX6 
ID   BOXA_AZOEV              Reviewed;         414 AA.
AC   Q9AIX6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   05-DEC-2018, entry version 84.
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   Azoarcus evansii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Zoogloeaceae; Azoarcus.
OX   NCBI_TaxID=59406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19 AND
RP   300-321, COFACTOR, SUBUNIT, AND INDUCTION.
RC   STRAIN=KB740 / DSM 6898;
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=KB740 / DSM 6898;
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
RT   Azoarcus evansii.";
RL   J. Bacteriol. 184:6301-6315(2002).
RN   [3]
RP   CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=KB740 / DSM 6898;
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
RT   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
CC       2,3-epoxy-2,3-dihydrobenzoyl-CoA. BoxA acts as a reductase that
CC       uses NADPH to reduce the oxygenase component BoxB. BoxAB does not
CC       act on NADH or 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
CC       BoxA/BoxB protein complex is not known.
CC       {ECO:0000269|PubMed:11222587}.
CC   -!- INDUCTION: By benzoate. {ECO:0000269|PubMed:11222587}.
DR   EMBL; AF220510; AAK00600.1; -; Genomic_DNA.
DR   EMBL; AF548005; AAN39377.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9AIX6; -.
DR   SMR; Q9AIX6; -.
DR   PRIDE; Q9AIX6; -.
DR   KEGG; ag:AAN39377; -.
DR   KO; K15511; -.
DR   BioCyc; MetaCyc:MONOMER-3142; -.
DR   BRENDA; 1.14.12.21; 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   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF13237; Fer4_10; 1.
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       Benzoyl-CoA oxygenase component A.
FT                                /FTId=PRO_0000350726.
FT   DOMAIN       12     41       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       42     70       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      143    265       FAD-binding FR-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00716}.
FT   NP_BIND     274    291       NADP. {ECO:0000250}.
FT   COMPBIAS    291    295       Poly-Arg.
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
//
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