ID A0A0D2CBM7_9EURO Unreviewed; 335 AA.
AC A0A0D2CBM7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_01498 {ECO:0000313|EMBL:KIW20919.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW20919.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW20919.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW20919.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847492; KIW20919.1; -; Genomic_DNA.
DR RefSeq; XP_016241135.1; XM_016375859.1.
DR AlphaFoldDB; A0A0D2CBM7; -.
DR STRING; 91928.A0A0D2CBM7; -.
DR GeneID; 27328581; -.
DR VEuPathDB; FungiDB:PV08_01498; -.
DR HOGENOM; CLU_031413_0_0_1; -.
DR OrthoDB; 2232005at2759; -.
DR Proteomes; UP000053328; 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:UP000053328}.
FT DOMAIN 14..119
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 143..207
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT REGION 316..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 36861 MW; 6D5B8555E997BA05 CRC64;
MSKDETTSCK TILAGTIAKG LLSEVQAGLS KLGRKPHLLG ILANADPAAK VYADWTEKTC
NDNGFAYTLK SVAKDDVEET IMAANNDDAV DGIIVYYPIF NNRQDQYLQQ IVDVSKDVEG
LSHQYIFNMY QNIRFLDESQ AIKSVLPCTP LAVIKILEFL HIYNTILPYG NRLFGRTICV
VNRSEVVGRP LAALLANDGA SVYSVDVTGV QLFTRGEGIR KRKHEVHEKE GWTLETCAPL
CDVVITGVPG DKFKFPCHLL KEGAVCINFS SEKNFPVEVK QKASIYVPAI GKVTIVVLLR
NLLRIVQNKQ ARLAQSHTTT VDGTQTEGGV DKATT
//
