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Database: UniProt
Entry: A7TQ26_VANPO
LinkDB: A7TQ26_VANPO
Original site: A7TQ26_VANPO 
ID   A7TQ26_VANPO            Unreviewed;       323 AA.
AC   A7TQ26;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   13-SEP-2023, entry version 73.
DE   RecName: Full=Methylenetetrahydrofolate dehydrogenase [NAD(+)] {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Kpol_489p12 {ECO:0000313|EMBL:EDO15631.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO15631.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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DR   EMBL; DS480451; EDO15631.1; -; Genomic_DNA.
DR   RefSeq; XP_001643489.1; XM_001643439.1.
DR   AlphaFoldDB; A7TQ26; -.
DR   STRING; 436907.A7TQ26; -.
DR   GeneID; 5543733; -.
DR   KEGG; vpo:Kpol_489p12; -.
DR   eggNOG; KOG0089; Eukaryota.
DR   HOGENOM; CLU_031413_0_0_1; -.
DR   InParanoid; A7TQ26; -.
DR   OMA; CKVITAE; -.
DR   OrthoDB; 2232005at2759; -.
DR   PhylomeDB; A7TQ26; -.
DR   Proteomes; UP000000267; 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:UP000000267}.
FT   DOMAIN          14..124
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          147..212
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   323 AA;  36378 MW;  21B9E572B3047380 CRC64;
     MSSSALKPGS TILASTVANN FGEEIIKKVD SLKSSLPNGP LLVGFLANND PAAEMYATWT
     KKSCESMGFR YELRRVEDRD FLEEAIIEAN RDDSVNGIMV YYPVFGNAQD QYLQQVVSRE
     KDVEGLNHVY YQNLYHNIRF LDSNNELKSI LPCTPLAVVK IMEYLKIYNT LLPEGNRLYG
     RKCVVINRSE IVGRPLAALL ANDGATVYSV DVNNIQKFTR GEGLKFTKHH VEDLGPYSED
     LLKKCCQDSD VIITGVPSES YKIPTEYIKD GTSCINFSSF RNFDDSVKTK ASLYVPMTGK
     VTIVMLLRNM LRLIENNQKL HGK
//
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