ID C1G4Z9_PARBD Unreviewed; 646 AA.
AC C1G4Z9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=PADG_02015 {ECO:0000313|EMBL:EEH45865.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH45865.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH45865.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH45865.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275958; EEH45865.2; -; Genomic_DNA.
DR RefSeq; XP_010757162.1; XM_010758860.1.
DR AlphaFoldDB; C1G4Z9; -.
DR STRING; 502780.C1G4Z9; -.
DR GeneID; 22581571; -.
DR KEGG; pbn:PADG_02015; -.
DR VEuPathDB; FungiDB:PADG_02015; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_17_5_1; -.
DR InParanoid; C1G4Z9; -.
DR OMA; LCCGGGC; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000001628; 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:UP000001628}.
FT DOMAIN 222..520
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 70904 MW; 6EB54332E40112EC CRC64;
MASSMTQHVE TIPISSTSHP DNPVPEEPTT LPHLKIMHPG TTSSPGTQTS SVSTIGTFDM
ASDSETPSTP ATEPLADEVI EGITDLTLSP KSPPLPTQHR RRRASTVLIS QSSHDVQKIL
GSSQGGTHVL EKLCCGGGCC KLQPLQEPAS SPLIHPVIKP KNKAFESLKL QLGKLSHDSA
LTNITPLPEK TVSFSPVPAE FAHEDLGPPD HPPRFVQPHP PYEVYRAPLR HARELTKPGA
EKRTYHFDID VTDYPAEGGN VDFVVGGAIG VCPQNSDEVV DNVFDLLNIP KMVRDRKVMV
RTTAGRWPTV WGDEKPRSLV TTRRQLLSWC SDLQSYPPTK QIFRLMAEYA TDRDEKKILM
FLSSAQGQGA FCDLRTDQHT TVSQLLSAFP SSQPPLDHLL STLNTLMPRF YSLSQDPLVS
CTLSDGKCQR LIEIAVTVHE APDWRGGNRT GVGSGFLERK AHQILEAEKS GKDILSLDLH
IPMFRGLMSN PLAREFVSDG PMLLIGAGVG VAPFRGFVQR RLKSANCANK VWVLQGIRDS
LLDELYSGEW GVHEETVKKV VQSRSGEGKY VQEEVRNQAD LVWFVINSLD GRVFVCGSSK
GMGEGVESAL VDVAMAKGNL NREEAQLFWQ GKKDAGQYIA LKRGNH
//
