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Database: UniProt
Entry: E3JWM7_PUCGT
LinkDB: E3JWM7_PUCGT
Original site: E3JWM7_PUCGT 
ID   E3JWM7_PUCGT            Unreviewed;       644 AA.
AC   E3JWM7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Methylenetetrahydrofolate reductase (NADPH) {ECO:0000313|EMBL:EFP76452.1};
GN   ORFNames=PGTG_02893 {ECO:0000313|EMBL:EFP76452.1};
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP76452.1, ECO:0000313|Proteomes:UP000008783};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CRL 75-36-700-3;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA   Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA   Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA   Schein J.;
RT   "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT   700-3.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL
RC   {ECO:0000313|Proteomes:UP000008783};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU004254}.
CC   -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC       {ECO:0000256|ARBA:ARBA00006743}.
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DR   EMBL; DS178265; EFP76452.1; -; Genomic_DNA.
DR   RefSeq; XP_003320871.1; XM_003320823.2.
DR   AlphaFoldDB; E3JWM7; -.
DR   STRING; 418459.E3JWM7; -.
DR   EnsemblFungi; EFP76452; EFP76452; PGTG_02893.
DR   GeneID; 10534508; -.
DR   KEGG; pgr:PGTG_02893; -.
DR   VEuPathDB; FungiDB:PGTG_02893; -.
DR   eggNOG; KOG0564; Eukaryota.
DR   HOGENOM; CLU_025841_2_2_1; -.
DR   InParanoid; E3JWM7; -.
DR   OMA; VARTSQW; -.
DR   OrthoDB; 1381745at2759; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IBA:GO_Central.
DR   GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR   CDD; cd00537; MTHFR; 1.
DR   Gene3D; 3.20.20.220; -; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR004621; Fadh2_euk.
DR   InterPro; IPR003171; Mehydrof_redctse-like.
DR   NCBIfam; TIGR00677; fadh2_euk; 1.
DR   PANTHER; PTHR45754; METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR45754:SF3; METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   Pfam; PF02219; MTHFR; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT   REGION          608..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   644 AA;  72636 MW;  CCE9B55DB0834E44 CRC64;
     MKISQKLAAA ESENRISWSF EYFPPKTDNG LTNLYDRICR MSQLGPIFID ITWGAGGSTS
     NLTTEFVKTA HEQFGLETCM HLTCTNMPKS KIDTALKEAY EFGCENILAL RGDPPKGSTE
     WTATEGGFEH AIDLVRHIRA EYGDHFDIAV AGFPEGHMHS TLSREQQTIY LKEKIEAGAN
     FIFTQMFYDV DIFIDWVREI RAAGITVPVI PGLMPIQSWA QFKRVTNFSK TIVPQYFLDK
     LEPIQSDDQA VREAGTKLVA DMCRKILNSD LGIRILHFYT MNLERGTKMI LDELNLNPSR
     DITNPLPWKM SLLGKRRSES IRPIFWANRA KSYLSRTETW DEFPNGRWGD SRSPAYGELD
     GYGININAAT METLKGLKKF PTSLADLARI FANYCGARFP GEEPVKYLPW SDIPLSEETN
     KIEDVLVKIN KRGFLTINSQ PAVDGAKSSD PVHGWGPRGG YVYQKAYLEF FCCPEKFQSL
     TERLEKDPDV TYYAVTKTGD LVTNNTRPGP NAVTWGVFPG KEIVQPTIVE LVSFIAWKDE
     AFELGHQWAE LYKEIAPESA RFIHQIMDSW YLVNIVNNDF RKSNDDSEHS ALFQFFGPEP
     VIVDQDDLPP TTNGLSHPNG LPKTNGSSTP AISEVNGELK NLAI
//
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