ID A0A0C4YVM3_9BURK Unreviewed; 426 AA.
AC A0A0C4YVM3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Benzoyl-CoA oxygenase component A {ECO:0000256|PIRNR:PIRNR000361};
DE EC=1.14.13.208 {ECO:0000256|PIRNR:PIRNR000361};
GN ORFNames=RR42_s3010 {ECO:0000313|EMBL:AJG24591.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG24591.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG24591.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG24591.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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:0000256|PIRNR:PIRNR000361};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000361}.
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DR EMBL; CP010537; AJG24591.1; -; Genomic_DNA.
DR RefSeq; WP_043356813.1; NZ_CP010537.1.
DR AlphaFoldDB; A0A0C4YVM3; -.
DR STRING; 68895.RR42_s3010; -.
DR KEGG; cbw:RR42_s3010; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000031843; Chromosome secondary.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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 NCBIfam; TIGR03224; benzo_boxA; 1.
DR PANTHER; PTHR43314; -; 1.
DR PANTHER; PTHR43314:SF27; FERREDOXIN--NADP REDUCTASE, LEAF ISOZYME 2, CHLOROPLASTIC; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF14697; Fer4_21; 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; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|PIRNR:PIRNR000361};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000361};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|PIRNR:PIRNR000361, ECO:0000256|PIRSR:PIRSR000361-1};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000361};
KW Reference proteome {ECO:0000313|Proteomes:UP000031843}.
FT DOMAIN 10..39
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 41..68
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 153..275
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 235
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 349..350
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 356
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 385..386
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 424
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ SEQUENCE 426 AA; 46206 MW; F2DDAC4EC49B20DC CRC64;
MDMSDIQVIR QHLIDPEICI RCNTCEATCP VAAITHDARN YVVDADKCNG CMACISPCPT
GSIDNWRTMP RAMAYGIVEQ FGWDTLPDEL SSEQLAAQGV AADAEPVLES APASSLAAVT
GEDGFNSAQY GATVPPWSAA HAYTNLYGAK AAARSVTATV VGNARVTEVG RDYDTHHIVL
DFGSAPFPVL EGQSIGIVPP GVDASGRQHH ARQYSLASPR NGERPGYNNI SLTIKRVLED
HQGNPVRGVA SNYMCDLQVG DKVDVIGPFG ASFLMPNHPR SHIVMICTGT GSAPMRAMTE
WRRRLRKSGK FEGGKLMLFF GARTQEELPY FGPLQSLPKD FIDINFAFSR TPGQPKRYVQ
DVMRERAADL GPLLADPNTC FYVCGLKSME EGVVLALRDV AQQAGLSWDA VGAALKKEGR
LHLETY
//
