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Database: UniProt
Entry: A0A151GUH7_9HYPO
LinkDB: A0A151GUH7_9HYPO
Original site: A0A151GUH7_9HYPO 
ID   A0A151GUH7_9HYPO        Unreviewed;       341 AA.
AC   A0A151GUH7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000313|EMBL:KYK60672.1};
GN   ORFNames=DCS_01810 {ECO:0000313|EMBL:KYK60672.1};
OS   Drechmeria coniospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX   NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK60672.1, ECO:0000313|Proteomes:UP000076580};
RN   [1] {ECO:0000313|EMBL:KYK60672.1, ECO:0000313|Proteomes:UP000076580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK60672.1,
RC   ECO:0000313|Proteomes:UP000076580};
RX   PubMed=26975455; DOI=10.1038/srep23122;
RA   Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA   Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA   Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA   Molnar I., Lin M.;
RT   "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT   Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL   Sci. Rep. 6:23122-23122(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYK60672.1}.
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DR   EMBL; LAYC01000001; KYK60672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151GUH7; -.
DR   STRING; 98403.A0A151GUH7; -.
DR   InParanoid; A0A151GUH7; -.
DR   OrthoDB; 2232005at2759; -.
DR   Proteomes; UP000076580; Chromosome 01.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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:UP000076580}.
FT   DOMAIN          14..126
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          149..215
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   341 AA;  37515 MW;  5C8B4C8FFA91186C CRC64;
     MASQDVPKTC KVITADTIAK GLLAEVKETL ARVQVPNGAE PTLAAFLANG DPAAVKYAEW
     SKKTCEENGF KFDLRTVDKE SLEEEIMRAN EDDDIDGTIV YYPVFPQNPI HDKYVQETVD
     LSKDVEGMRH MHLHNMYHNV RFLDAPENKK KSILPCTPLA VVKILEHLQI YNLILAPGNR
     LFGKTITVIN RSEVNGRPLA ALLANDGATV YSVDVTGVQL FTRGQGIKHP RHQVEDKEGW
     GLEECLPLSD VVIGGVPAES FKVPTELIRD GAVCINFSSH KNFDGPAIKE KASIYVPSVG
     KVTIAVLLRN LVRLIANRPS KDGTAEGVIQ AKSEAFVDDY A
//
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