ID A0A0D2ENP5_9EURO Unreviewed; 704 AA.
AC A0A0D2ENP5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=PV05_11129 {ECO:0000313|EMBL:KIW49454.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW49454.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW49454.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW49454.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KN847323; KIW49454.1; -; Genomic_DNA.
DR RefSeq; XP_013310039.1; XM_013454585.1.
DR AlphaFoldDB; A0A0D2ENP5; -.
DR STRING; 348802.A0A0D2ENP5; -.
DR GeneID; 25333037; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT DOMAIN 283..555
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 76..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 77769 MW; 6FA988736A2046A1 CRC64;
MDCQSSITRL HNAAKSPSLL QLNGLTSMLR TFRKRIPSFF LQPTNIHIST GARLGIPFRY
TMASLNTMAA GHEVPLTAHS HPHNPIPEDP TRTRKVSIST SQFGRSPMST ATTGTYSDNE
ASSIDTTPTT PTDNLSDDSF NEQQDRTYSK PQPKQRRAST VLVSEDSEDA RRFLGQAGTA
TSMVQKACCG GGCCMLQELK FKGAAEGVKP IREPDNAAYR SLKLKLGALS LDSELTGIVD
MPAKTVSLES LSTSSNTTYA QPPKKTTEVL KHPPNFVTPH PPYQVYSAPL FHARELTKSG
AEKRTYHFDI DVTDYPTEGG DVDFVVGGAI GVCAPNSPEM VNKVFDALGV PSFVRDKPVL
LKTTTGRWPT IWGDDAPREL VTTRRELLTW CSDIQSYAPT KQLFRLLAEY AEDEHEKMIL
MYLSSAQGQG AFCDLRTGPY TTIPQLLTAF PSTRPPLDYL LSVLNQLMPR FYSLSQDPMV
SCQRDSTERR RLVEIAVSVH EAEDYATGMR TGVGSGFLER LARQVIEAEK AGKDPKDLDL
RIPMFRGLMA NPLAREFVTD GPMLLIGAGV GIAPFRGFVH RRLKSANCAN KVWVLQGIRD
SLLDELYSGD WGVHEDKVKK VVQSRRGEGR YVQEEVRHQA DLVWFIINAL DGRIFVCGSS
KGMGEGVEAA LIDVAMAKGK LNQEEAKSFW AEKKASGQYI AETW
//
