ID F7SVN7_9BURK Unreviewed; 414 AA.
AC F7SVN7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Benzoyl-CoA oxygenase component A {ECO:0000256|PIRNR:PIRNR000361};
DE EC=1.14.13.208 {ECO:0000256|PIRNR:PIRNR000361};
GN ORFNames=AXXA_03659 {ECO:0000313|EMBL:EGP47818.1};
OS Achromobacter insuavis AXX-A.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP47818.1, ECO:0000313|Proteomes:UP000004853};
RN [1] {ECO:0000313|EMBL:EGP47818.1, ECO:0000313|Proteomes:UP000004853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AXX-A {ECO:0000313|EMBL:EGP47818.1,
RC ECO:0000313|Proteomes:UP000004853};
RA Bador J., Amoureux L., Neuwirth C.;
RL Submitted (JUN-2011) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGP47818.1}.
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DR EMBL; AFRQ01000028; EGP47818.1; -; Genomic_DNA.
DR RefSeq; WP_006390781.1; NZ_GL982453.1.
DR AlphaFoldDB; F7SVN7; -.
DR PATRIC; fig|1003200.3.peg.702; -.
DR eggNOG; COG0369; Bacteria.
DR eggNOG; COG1149; Bacteria.
DR HOGENOM; CLU_053066_0_0_4; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000004853; Unassembled WGS sequence.
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; 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; PF12838; Fer4_7; 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}.
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 143..265
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 191..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 280
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 337..338
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 344
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 373..374
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 412
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ SEQUENCE 414 AA; 45526 MW; 5AB5EC585F024212 CRC64;
MNAALPVEVL KQHLIDPEIC IRCNTCEETC PIDAITHDSN NYVVDPEICN GCMACVPPCP
TGSIDNWRLV VRAEAYSLQD QLGWDELPHE QPLPDAAVAA QAEADATLEP APAATVAMPA
ATPGASVPPW SAAHPYVNLY THKTPVTATV VGNYRVTGAD TDSDIHHIVL DFGELPFPVL
EGQSIGILPP GADAQGRPHH ARQYSLASPR DGERAGYNNL SLTVKRVTED HQGQSAYGVC
SNYLCDLAKN DTVQVIGPFG HTFLMPNHPR ANLIMICTGT GSAPMRAMTE RYRRRIETGE
NGRLLLFFGA RTERELPYFG PLMKLPRDFI DINLALSRES GQPKRYVQDL IRERAAAVRE
LLADRNTCIY VCGLKGMEVG VLDALREVAV QAGQDWTILH DVLRREGRLH FETY
//
