ID A0A137PDI0_CONC2 Unreviewed; 305 AA.
AC A0A137PDI0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=NAD(P)-binding protein {ECO:0000313|EMBL:KXN72991.1};
GN ORFNames=CONCODRAFT_55809 {ECO:0000313|EMBL:KXN72991.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN72991.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN72991.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN72991.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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DR EMBL; KQ964443; KXN72991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137PDI0; -.
DR STRING; 796925.A0A137PDI0; -.
DR EnsemblFungi; KXN72991; KXN72991; CONCODRAFT_55809.
DR OMA; CKVITAE; -.
DR OrthoDB; 2232005at2759; -.
DR Proteomes; UP000070444; Unassembled WGS sequence.
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:UP000070444}.
FT DOMAIN 8..113
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 135..200
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 305 AA; 34467 MW; 380EDC74F3D9F62B CRC64;
MPGHQVNSST IAVKYRDEIK NTINSKNIRP KLVSFLANED PAAQMYANWT AKTCAESGIE
FECRKVDKKD LEDKIVEANE DNNIHGIMVY YPVYGDRQDQ YLQSVVSEKK DVEGLCHKYV
YNMYHNVRFL DDENTKKCII PCTPLAVVKI LEAVGVYNTV LPYGNRLHGK TIAVINRSEV
VGRPLAALLA NDGARVFSVD INDILEFNRG AGLKMSKHQV SETDYKLEDI LPKCDVVITG
VPTPNYQVNT ELLKEGVVAI NFSSHKNFAP DIKERASIYV PSIGKVTIAM LERNLLRLYD
YYNKQ
//
