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Database: UniProt
Entry: G8B9E8_CANPC
LinkDB: G8B9E8_CANPC
Original site: G8B9E8_CANPC 
ID   G8B9E8_CANPC            Unreviewed;       322 AA.
AC   G8B9E8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=CPAR2_302370 {ECO:0000313|CGD:CAL0000147627,
GN   ECO:0000313|EMBL:CCE41248.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE41248.1, ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA   Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT   response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(2011).
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DR   EMBL; HE605204; CCE41248.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8B9E8; -.
DR   STRING; 578454.G8B9E8; -.
DR   EnsemblFungi; CPAR2_302370-T; CPAR2_302370-T-p1; CPAR2_302370.
DR   CGD; CAL0000147627; CPAR2_302370.
DR   VEuPathDB; FungiDB:CPAR2_302370; -.
DR   eggNOG; KOG0089; Eukaryota.
DR   Proteomes; UP000005221; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; IEA:EnsemblFungi.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:EnsemblFungi.
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:UP000005221}.
FT   DOMAIN          11..116
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          139..211
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   322 AA;  36350 MW;  82295FDB3922E495 CRC64;
     MSRPAGRTIL ASTIAKPFQE EVISAVKKLN FKPTLVGLLA NEDPAAKMYA NWTSKTCESL
     GFNYKLIEVN KNELETSLIK ANRDDDVNGI MVYFPVFGDK QDQYLQQLIS PEKDVEGLNF
     LYYHNLYHNV RFLDPPRNQQ KSILPCTPLA MVKILEYLGV YNKILPYGNR LYGKKILVVN
     RSEIVGRPLA ALLANDGATV YSVDINNIQQ FTRGDDLSEH RHLVVDLNGD DYTVEKLAPQ
     CDVIITGVPS ENYKFPTNLV RHGTIVINFS SSKNFDDEIK QKAGLYVPSI GKVTIAILLR
     NLIRLIDNKK IRANEANEET SR
//
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