ID A0A0D2EPQ0_9EURO Unreviewed; 1055 AA.
AC A0A0D2EPQ0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=PV05_11435 {ECO:0000313|EMBL:KIW49789.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW49789.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW49789.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW49789.1,
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; KIW49789.1; -; Genomic_DNA.
DR RefSeq; XP_013310373.1; XM_013454919.1.
DR AlphaFoldDB; A0A0D2EPQ0; -.
DR STRING; 348802.A0A0D2EPQ0; -.
DR GeneID; 25333343; -.
DR HOGENOM; CLU_003662_1_0_1; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 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; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF01558; POR; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52922; TK C-terminal 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 667..898
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1055 AA; 116271 MW; CACDD57AC6718960 CRC64;
MASSQSQSFG QSPPLSSVAG PTYVTAQTLV QQVAYTLSDK IFSYSPETFD LDIAARAWAE
AQETNANGYK TAVQSMQIRN GAGSIALGYM FSKDFDLKKR HIPQGLLAPS SALTFLRPVL
DQLSLLYSVS NPFVAHIAAL DYEGEKNGEL VSDYASALST AEDLGLGLVA SQSAHEAQHM
SLLATLLARD LPTLHVYDGL RVGRDTTRVI DILDKSGLGA AYQSVLESIS DEDRKHLSPE
GKALKTLRAL NEELGTDYKA FEYFGHEQPE VVLVAFGSVE SSLAAQAATA LARSGNRIGT
INVRLYRPFA EEQFLHLLPI GVRVVGVLGQ VLDAQAVQDA GLHSQLYEDV LASVSYGTSI
QNTPEVRELK YARAERWTPS SISATFQMLL GKPADDQGVT TFLDDSVQQY TFWNADDAPS
ASAATYLAQA LAKDSAQNVT VNTTHDNLLQ GGSYRIEIRK SPKTIDASYP ISSANTAVVT
DVKLLEKVDV LKSVSKGGNL LLLLPGVKDE DVEKKLPAAF KKSVAETGVG LYLINPGNTA
LNTENSSELE SLMLQTAFLR VALGKSEEIG LQKLATINSD IKLLEEVASD LEKTLRQIEV
PKEWAEVEVE PTKEALPTDM LSNSFVSFDK TEEEPPSVLR SWQKAAKGLL FKEAYSTENA
LRPELPTKTF TVHVKENRRL TPVTYERNIF HIEFDLGTSG LKYDIGEALG VHAENDHDQV
MDFIRWYGLN HEDVVEVASR EDPAIFENRT VYQALLQNVD IFGRPQKKFY EALADFADDE
NEKKVLLTLA GPEGFKEFQR RAEVDTVTFA DILLEFPSAH PSFHEIVRIV PPMKRREYSI
ASCQAVTPTS VALMVVVVNW VDPKGRDRFG QATKYLSSLK VGTSVTVSVK PSVMKLPPKS
TQPIIMAGLG TGLAPFRAFV QHRAMEKAQG KEIGAVLLYM GSRHQREEYC YGEEWEAYQA
AGVITLLGRA FSRDQPQKIY IQDRMRQTLD DITKAYIKEE GAFYLCGPTW PVPDVTNVLE
EAIAKEAKAS GAKKVDPSRE IMKLKDEGRY VLEVY
//
