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Database: UniProt
Entry: K1V0E7_TRIAC
LinkDB: K1V0E7_TRIAC
Original site: K1V0E7_TRIAC 
ID   K1V0E7_TRIAC            Unreviewed;       350 AA.
AC   K1V0E7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Methylenetetrahydrofolate dehydrogenase (NAD+) {ECO:0000313|EMBL:EKC97399.1};
GN   ORFNames=A1Q2_08322 {ECO:0000313|EMBL:EKC97399.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC97399.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKC97399.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC97399.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
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:EKC97399.1}.
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DR   EMBL; AMBO01000412; EKC97399.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1V0E7; -.
DR   STRING; 1220162.K1V0E7; -.
DR   eggNOG; KOG0089; Eukaryota.
DR   HOGENOM; CLU_031413_0_1_1; -.
DR   InParanoid; K1V0E7; -.
DR   OMA; CKVITAE; -.
DR   OrthoDB; 2232005at2759; -.
DR   Proteomes; UP000006757; Unassembled WGS sequence.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
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; 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   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT   DOMAIN          15..129
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          170..233
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   350 AA;  38372 MW;  C8082A92A6CA8532 CRC64;
     MSSNNHQGIL VTASKVHVPF KAELLQAIND PRFQKRAPHL VGILATKKED ARSYAERACE
     QIGINFELRL VGQAREGMDG AGVGIGVEEA ILEANEDDDV DGIMVYYPIY GDRQDQYLQS
     VVSPVKDVEG LNHQFLFNLY HNIRFISPLT LRPVPGAIET GDQPPEGTVK SILPCTPLAI
     VKVLEHVGVY NSLIPYGDRA RGKVITVINR SEVVGRPLAA LLANDGARVF SVDITGIVEF
     SKRPSKQSKY NPHHVINPTD LSLEEVLGRS DVVISAVPSQ SYKVPTAQLK DGCVCVNVAG
     EKNFEADVRE RASIYVPSVG VMTIAMLQRN LLRLCKYQDM VKEATQAKSA
//
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