ID T1X3Q8_VARPD Unreviewed; 432 AA.
AC T1X3Q8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Benzoyl-CoA oxygenase component A {ECO:0000256|PIRNR:PIRNR000361};
DE EC=1.14.13.208 {ECO:0000256|PIRNR:PIRNR000361};
GN Name=boxA {ECO:0000313|EMBL:AGU47228.1};
GN ORFNames=VAPA_1c00970 {ECO:0000313|EMBL:AGU47228.1};
OS Variovorax paradoxus B4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1246301 {ECO:0000313|EMBL:AGU47228.1, ECO:0000313|Proteomes:UP000016223};
RN [1] {ECO:0000313|EMBL:AGU47228.1, ECO:0000313|Proteomes:UP000016223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:AGU47228.1,
RC ECO:0000313|Proteomes:UP000016223};
RA Schuldes J., Brandt U., Hiessl S., Wuebbeler J.H., Thuermer A.,
RA Steinbuechel A., Daniel R.;
RT "Genome sequence of Variovorax paradoxus B4.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP003911; AGU47228.1; -; Genomic_DNA.
DR RefSeq; WP_021004801.1; NC_022247.1.
DR AlphaFoldDB; T1X3Q8; -.
DR KEGG; vpd:VAPA_1c00970; -.
DR PATRIC; fig|1246301.3.peg.101; -.
DR HOGENOM; CLU_053066_0_0_4; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000016223; Chromosome 1.
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; 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; 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; 2.
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 ECO:0000313|EMBL:AGU47228.1}.
FT DOMAIN 11..40
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 42..69
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 159..281
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 241
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 296
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 355..356
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 362
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 391..392
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 430
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ SEQUENCE 432 AA; 46752 MW; 273AB80111F8F0AE CRC64;
MDMAVEAGVI KQHLIDPEIC IRCNTCEATC PVNAITHDDN NYVVRADVCN GCMACISPCP
TGSIDNWRTM PLVRAYTIEE QLTWESLPAE LSPEELEAAG VSAEAAGDAA AAVPAQTQAQ
AQAQAAVESV EPAFNSAQYG ASVPPWSAAH AYTNLFAPKA PTTATVVGNF NCTEAGFDSE
THHIVLDFGM VPFPVLEGQS IGIVPPGVDA IGKRHHARQY SVASPRNGER PGYNNVSLTV
KRVTEDHQGD PVRGVCSNYV CDLKVGDTVQ VVGPFGSSFL MPNHPRSHIV MICTGTGSAP
MRAMTEWRRR LRKSGKFEGG KLMLFFGART QQELPYFGPL QSLPKDFIDI NLAFSRTPGS
PKRYVQDLMR ERAADLAALL KDGSSHFYVC GLKSMEEGVV LALRDVAKEA GLDWDTVGAA
LKREGRLHLE TY
//
