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Database: UniProt
Entry: A7EQZ8_SCLS1
LinkDB: A7EQZ8_SCLS1
Original site: A7EQZ8_SCLS1 
ID   A7EQZ8_SCLS1            Unreviewed;       369 AA.
AC   A7EQZ8;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SS1G_07751 {ECO:0000313|EMBL:EDN91890.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN91890.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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DR   EMBL; CH476630; EDN91890.1; -; Genomic_DNA.
DR   RefSeq; XP_001591126.1; XM_001591076.1.
DR   AlphaFoldDB; A7EQZ8; -.
DR   STRING; 665079.A7EQZ8; -.
DR   GeneID; 5487451; -.
DR   KEGG; ssl:SS1G_07751; -.
DR   InParanoid; A7EQZ8; -.
DR   OMA; CKVITAE; -.
DR   OrthoDB; 2232005at2759; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IBA:GO_Central.
DR   CDD; cd01079; NAD_bind_m-THF_DH; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR035812; m-THF_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000672; THF_DH/CycHdrlase.
DR   InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR   InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR   PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR48099:SF3; METHYLENETETRAHYDROFOLATE DEHYDROGENASE [NAD(+)]; 1.
DR   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT   DOMAIN          59..165
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          189..255
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   369 AA;  41076 MW;  D899FA3C3EBE979F CRC64;
     MRKEDFLSAK QVHTRPLSKY CDYDIENCTT KSFAPNHSKY HREMASSPVP ATCKVILAQG
     IAKKLLGEVS TDLKKLSFKP KLVGLLANDD PAAQQYADWS MATCIENGFD FELRKFTKEE
     IEDEILKANN DDSIHGIIVY YPIFPAPSLQ DGYIQQIVAL NKDVEGLAHT YRFNMYQNIR
     FLDAPHNTQK SILPCTPLAV VKVLEHLQIY NSVLPYGNRL YGKTITVFNR SEVVGRPLAA
     LLANDGATVY SCDLDGVKLF TRGKGIKKVH HEVHDMEGMK NDDCLPKSDV VISGVPGERF
     KVNTELIRDG AVCINFSSQK NFDGPAVKEK ASIYVPSIGK VTIAVLLRNL LRLVENQGKG
     AAKPTEISN
//
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