ID V2J7T7_9BURK Unreviewed; 792 AA.
AC V2J7T7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:ESJ26292.1};
GN ORFNames=B551_0201595 {ECO:0000313|EMBL:ESJ26292.1};
OS Cupriavidus sp. HPC(L).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESJ26292.1, ECO:0000313|Proteomes:UP000053474};
RN [1] {ECO:0000313|EMBL:ESJ26292.1, ECO:0000313|Proteomes:UP000053474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA Purohit H.J., Agarwal L.;
RT "Cupriavidus a Desert isolate.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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:ESJ26292.1}.
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DR EMBL; AMPR02000011; ESJ26292.1; -; Genomic_DNA.
DR RefSeq; WP_006576905.1; NZ_AMPR02000011.1.
DR AlphaFoldDB; V2J7T7; -.
DR OrthoDB; 544091at2; -.
DR Proteomes; UP000053474; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11078; CYP130-like; 1.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46696:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022643};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000053474}.
FT DOMAIN 476..579
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 705..792
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 88254 MW; F9C4E9DE87EB48D9 CRC64;
MSERTEPAHA QGCPFHVQPH GQANASADAV ATPLSPTGCP VSARAADFDP FEDGYQQDPP
DYVRWAREQE PVFYSPRLGY WVVTRYDDIK AIFRDNLTFS PSIALEKITP TGDEANAVLA
SYGYAMNRTL VNEDEPAHMP RRRVLMEPFT PEQLQHHEPM VRRLTREYVD RFIDDGKADL
VDQILWEVPL TVALHFLGVP EEDMDLLRKY SIAHTVNTWG RPKPEEQVEV AHAVGNFWQL
AGRILDKMRQ DPSGPGWMQY GIRKQKEYPD VVTDSYLHSM MMAGIVAAHE TTANASANAI
KLLLQHPDAW RELCEDPSLI PNAVEECLRH NGSVAAWRRL ATRDVQIGGV DIPAGAKLLI
VTSSANHDER HFADADLFDI RRANASDQLT FGYGAHQCMG KNLARMEMQI FLEEFTRRLP
HMKLSEQTFT YVPNTSFRGP EHLWVEWDPS QNPERRNPAL LQVRTPVRIG EPSSHAINRT
VVVESMTRVA DDIVRLRLVS PDGKPLPRWS PGSHIDVECG DTGVSRQYSL CGDPADSRAF
EIAVLREADS RGGSAWIHRE LKAGDRLRIR GPRNHFRLDE SARRLILIAG GIGITPISAM
ARRAKELGID YQLHYCGRGR ASMALLDELA ALHGERLHVY ARDEGARADL GALLGQPDAA
TQIYACGPAR MLDALAACCA DWPEDALRVE HFTSTLGALD PSKEQAFEAE LKDSGIVVAV
RADQTLLAAL RAANIDVQSD CEEGLCGSCE VRVLAGDIDH RDVVLTRAER EANSKMMSCC
SRARCGRIVL EL
//
