ID A0A0D3V954_9BACL Unreviewed; 1066 AA.
AC A0A0D3V954;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0000256|PIRNR:PIRNR000209};
DE Includes:
DE RecName: Full=Cytochrome P450 {ECO:0000256|PIRNR:PIRNR000209};
DE EC=1.14.14.1 {ECO:0000256|PIRNR:PIRNR000209};
DE Includes:
DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|PIRNR:PIRNR000209};
DE EC=1.6.2.4 {ECO:0000256|PIRNR:PIRNR000209};
GN ORFNames=UB51_10470 {ECO:0000313|EMBL:AJS58829.1};
OS Paenibacillus sp. IHBB 10380.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566358 {ECO:0000313|EMBL:AJS58829.1, ECO:0000313|Proteomes:UP000032320};
RN [1] {ECO:0000313|EMBL:AJS58829.1, ECO:0000313|Proteomes:UP000032320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHBB 10380 {ECO:0000313|EMBL:AJS58829.1,
RC ECO:0000313|Proteomes:UP000032320};
RX PubMed=25908145;
RA Pal M., Swarnkar M.K., Thakur R., Kiran S., Chhibber S., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequence of Paenibacillus sp. Strain IHBB 10380 Using
RT PacBio Single-Molecule Real-Time Sequencing Technology.";
RL Genome Announc. 3:0-0(2015).
CC -!- FUNCTION: Functions as a fatty acid monooxygenase.
CC {ECO:0000256|PIRNR:PIRNR000209}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036596,
CC ECO:0000256|PIRNR:PIRNR000209};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209,
CC ECO:0000256|PIRSR:PIRSR000209-1};
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018, ECO:0000256|PIRNR:PIRNR000209}.
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DR EMBL; CP010976; AJS58829.1; -; Genomic_DNA.
DR RefSeq; WP_044877246.1; NZ_CP010976.1.
DR AlphaFoldDB; A0A0D3V954; -.
DR STRING; 1566358.UB51_10470; -.
DR KEGG; pih:UB51_10470; -.
DR PATRIC; fig|1566358.3.peg.2336; -.
DR HOGENOM; CLU_001570_7_0_9; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000032320; Chromosome.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-UniRule.
DR CDD; cd06206; bifunctional_CYPOR; 1.
DR CDD; cd11068; CYP120A1; 1.
DR Gene3D; 3.40.50.360; -; 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; IPR023206; Bifunctional_P450_P450_red.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00067; p450; 1.
DR PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000209};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000209};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000209};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR000209};
KW Heme {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW Iron {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000209,
KW ECO:0000256|PIRSR:PIRSR000209-1};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|PIRNR:PIRNR000209};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000209};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000209};
KW Reference proteome {ECO:0000313|Proteomes:UP000032320};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000209}.
FT DOMAIN 497..637
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 676..909
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000209-1"
SQ SEQUENCE 1066 AA; 120406 MW; 99AB4FCB1F8FA072 CRC64;
MDNNKNPQIP QPKTFGPLGN LPQLNIEEPV QSMVRLADEF GPIFRMDYPG GRSEIYISDQ
DLVADACDES RFDKKVWAPL QKVSAFTGDG LFTSATEEPN WQKAHNILLP SFSQRAMQGY
HNMMVDIAVQ LVQKWARLNP DESVNVPEDM TRLTLDTIGL CGFDYRFNSF YRDQPHPFIV
SMVRALDEAM SQLTRLGIQD KLMPMTKRQF KRDIEAINSL VDNIIAERRL SGNQDAEDLL
SRMLNNKDPE TGEGIDDENI RYQIITFLIA GHETTSGLLS FAIYYLLNNL DKLHKAYEEV
DRVLTDSTPT YKQVLDLKYI RMILSETLRL WPTAPAFSLF AKEDTILAGR YPLKKGESVN
VLIPKLHRDT NAWGDDVEDF RPERFEDQSQ VPQDAYKPFG NGQRACIGQQ FALHEAVLVL
GMVLKHFELI DHTHYQLKVK ETLTLKPDNF TIHVRSRQPM ELNMSVADKS SSTGKDDNRT
NQEPQSVSII GASHLSLLVL YGSNLGTAEG IARELADTAR FYGVRSEVDT LNNRIGKLPK
EGAAVFIVTA SYNGKPPSNA SEFVQWLERV EPGELEGVNY VVFGCGDRNW ASTYQDVPKF
IDKQLADKGA RRLSLRGEGD ASGDFEKELE DWRDRLWPDV MEAFELKFNE KMDKERSSLT
VQFVSGLAGA PLAQSYEAVH ATVTENNELQ LVNTGRSTRH IEITLPEGVT YQEGDHLGVL
PSNSREIVDR VLRRFGLNGN DQLVVKASGR SSAHLPLDSP VSLYDLLSHS VELQEAATRA
QLRELMVVTV CPPHKHEIEA LLEEEAYKEQ VLKKRISMLD ILEKYEACEM SFERFLELLP
PLKARYYSIS SSPRLTPERS SITVAVVQGP AWSGHGEYRG VTSNYLADRK PGDDIVMFVR
TPESGFQLPE DTETPIIMVG PGTGVAPFRG FLQARAALKQ EGKTLGAAHL YFGCRTEDDF
IYREELEQYE RDGVVTLHTA FSRKGQDEKT YVQHLMNKNK EELIDILDHN GRLYICGDGS
KMAPDVEKTL QEAYQEVHTV DEQEAKAWLD GLQNEGRYAK DVWAGI
//
