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Database: UniProt
Entry: W2KF87_PHYPR
LinkDB: W2KF87_PHYPR
Original site: W2KF87_PHYPR 
ID   W2KF87_PHYPR            Unreviewed;       698 AA.
AC   W2KF87;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Methionine synthase reductase {ECO:0000256|ARBA:ARBA00040659};
DE            EC=1.16.1.8 {ECO:0000256|ARBA:ARBA00039088};
GN   ORFNames=L917_16326 {ECO:0000313|EMBL:ETL83773.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL83773.1};
RN   [1] {ECO:0000313|EMBL:ETL83773.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL83773.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; KI681972; ETL83773.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2KF87; -.
DR   EnsemblProtists; ETL83773; ETL83773; L917_16326.
DR   VEuPathDB; FungiDB:PPTG_16570; -.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.360; -; 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; IPR003097; CysJ-like_FAD-binding.
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:SF84; METHIONINE SYNTHASE 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   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
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; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          27..171
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          286..541
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   698 AA;  78009 MW;  877A017042535571 CRC64;
     MYLEKNLWPT KSSHQLPRTS AMASRAVSVF YGSQTGCAES IAQRIYDEAL EKQLDAELHP
     LNEFQKSKVE TCDGHFVVIV CSTTGNGDPP DNCGKFWRYV KRRTQPEDML AKLRYTVLGL
     GDTNYDKFCF MGKSIEKRMR ELGAQSFYEF GAADEAMGLE DSVEPWLNGL WEAFDKANGV
     IEVTADVVTS VSDIKESTAN RGNATNSLTT EKTSSTSTTV NTPYILDNLI SYEKMFGPLD
     TPTEVPEDLP RLQHSLLSVH FLGDEERQKP IHTSTTDEDD KEISSTNPFM ASLIGAEYLT
     APHAERKVLR LDIDVSGSGI QYVPGDSIGI KCPNRTEDVD ALLARLGVSG DEVFSAEPVA
     ATNGRAAKRK NTSIHFPTPC SVRDVFLHYV DILSSPKKAA VRALATYCTD EEERARMLLL
     SSKTGADKYT EFITEQHLNF AEILHFFPSC KPPLDHLLTL IPQLMPRYYS IATSPLVDPT
     RLSVAFTVVE YAVGEQRLRR RGLCTNWLNK ICQPLIGASV AASITIKIPI FLRGTQDFHL
     PENSQSPMVL IGPGTGVAPF MGFLQHRYYE AKDASVTRGD AYLFFGCRRQ SEDWLFKEQM
     QEYASNGTLR QLFTAFSRDQ DEKHYVQHDL RDNVELVADI LLGSDGYVFV CGDGMAMAKD
     VHTALVGILT ERAGLSQEDV ELKLRELGTQ HRYVRDIW
//
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