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Database: UniProt
Entry: G9P945_HYPAI
LinkDB: G9P945_HYPAI
Original site: G9P945_HYPAI 
ID   G9P945_HYPAI            Unreviewed;       338 AA.
AC   G9P945;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIATDRAFT_85094 {ECO:0000313|EMBL:EHK41072.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK41072.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK41072.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
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:EHK41072.1}.
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DR   EMBL; ABDG02000027; EHK41072.1; -; Genomic_DNA.
DR   RefSeq; XP_013939464.1; XM_014083989.1.
DR   AlphaFoldDB; G9P945; -.
DR   STRING; 452589.G9P945; -.
DR   GeneID; 25785869; -.
DR   eggNOG; KOG0089; Eukaryota.
DR   HOGENOM; CLU_031413_1_1_1; -.
DR   OMA; CKVITAE; -.
DR   OrthoDB; 2232005at2759; -.
DR   Proteomes; UP000005426; Unassembled WGS sequence.
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:UP000005426}.
FT   DOMAIN          13..126
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          149..216
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   338 AA;  37632 MW;  DAA86EED470C4B17 CRC64;
     MASEVAPKTC KVITAETIAK KLLLEVKDTL SKVQEAGSSA PTLVAFLAND DPAAVQYAEW
     SKKTCEENGF NFELRRVDKD VLEEDIMRAN EEDAVDGILV YYPIFPKNPS QDKYVQETVD
     LTKDVEGMRH TYLHNMYHNI RFLDPPENKK KSILPCTPLA VVKILEHLQI YNPILAYGNR
     LFGKTITVIN RSEVNGRPLA ALLANDGATV YSVDITGVQL FTRGQGIKKI RHQVEDKEGW
     GLEQCLPLSD VIIGGVPVES YKIPTELIRE GAVCINFSSF KNFDGVAVKE KASIYVPSVG
     KVTIAILLRN LVRLVANRPP KEDKSTIQAR TEAFADEI
//
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