ID H6C3F5_EXODN Unreviewed; 644 AA.
AC H6C3F5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=[methionine synthase] reductase {ECO:0000313|EMBL:EHY58170.1};
GN ORFNames=HMPREF1120_06184 {ECO:0000313|EMBL:EHY58170.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY58170.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY58170.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY58170.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) 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; JH226134; EHY58170.1; -; Genomic_DNA.
DR RefSeq; XP_009158631.1; XM_009160383.1.
DR AlphaFoldDB; H6C3F5; -.
DR STRING; 858893.H6C3F5; -.
DR GeneID; 20310823; -.
DR VEuPathDB; FungiDB:HMPREF1120_06184; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_17_5_1; -.
DR InParanoid; H6C3F5; -.
DR OMA; LCCGGGC; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000007304; 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:UP000007304}.
FT DOMAIN 223..490
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 71038 MW; 6D84C8073E6DFC6D CRC64;
MFTSSTTTPR HPLPLAPHSH PNNPIPEDPT RSRKLSVTAS QLSRSSASTM TNTAYSDDAS
SIDTAPTTPI TEALSDDSLD EMQDKSKANA APRQRRASTL LVSEDSEDAR RFLGETGTAT
RMIQKACCGG GCCMLQELNL STASPGENPI KPPDNSAFRS LKLKLAGLSL DSELTAIIDL
PPKTVSLEAL STSRPSTYAA SQPKPTTETL RHPPNFVTPH PPYQVFSAPL YSARELTKPG
AEKRTYHFDI DVTDYPEEGG NVDFVVGGAI GVCAPNHPEV VEQVFQQLGI PKFVRDKLVL
LKTTSGRWPT IWGEDEAREL VTTRRELLTW CSDLQSYPPT KQLLRVLAEY AEEQHEKKIL
MYLCSAQGQG AFCDLRTGPY ITIPQLLDAF PSSKPPLEYL FSVLNQLMPR FYSLSQDPII
SSERNGDGSR RLIEIAVTVH EAPDYRGGSR TGVGSGFLER LARKFIEAEQ QGKNARELDL
RIPMFRGLMA NPLAREFVTD GPMLLIGAGV GVAPFRGFVH RRLKSANCAN KVWVLQGVRD
SLLDELYSGD WGVHEDKVKK VVQSRRGEGK YVQEEVRAQA DLVWFIINAV DGRIFVCGSS
KGMGEGVENA LVDVAMAKGK LNREEAHAFW DEKKKSGQYI AETW
//
