ID C4YNB3_CANAW Unreviewed; 1024 AA.
AC C4YNB3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=C-1-tetrahydrofolate synthase, mitochondrial {ECO:0000313|EMBL:EEQ43146.1};
GN ORFNames=CAWG_01369 {ECO:0000313|EMBL:EEQ43146.1};
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ43146.1, ECO:0000313|Proteomes:UP000001429};
RN [1] {ECO:0000313|EMBL:EEQ43146.1, ECO:0000313|Proteomes:UP000001429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1 {ECO:0000313|EMBL:EEQ43146.1,
RC ECO:0000313|Proteomes:UP000001429};
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).
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC formate--tetrahydrofolate ligase family.
CC {ECO:0000256|ARBA:ARBA00006985}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000256|ARBA:ARBA00005559}.
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DR EMBL; CM000309; EEQ43146.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YNB3; -.
DR PaxDb; 5476-C4YNB3; -.
DR VEuPathDB; FungiDB:CAWG_01369; -.
DR HOGENOM; CLU_003601_2_0_1; -.
DR OMA; IKRVVDC; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001429; Chromosome R.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00477; FTHFS; 1.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR Gene3D; 1.10.8.770; -; 1.
DR Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01543; FTHFS; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR000559; Formate_THF_ligase.
DR InterPro; IPR020628; Formate_THF_ligase_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR PANTHER; PTHR48099:SF5; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR Pfam; PF01268; FTHFS; 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.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00721; FTHFS_1; 1.
DR PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 71..196
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 200..363
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 1024 AA; 111202 MW; 2B2D6F7F988D6FCE CRC64;
MTHRKNYTDT AYTRLKNFVM LFLKKRTTIF FFFLFFSLSI PPAMLRLRPT IRSLSRNFHR
SCINLDAVVV SGTKLANTIR ANVAEKVINY NKEHFGDNNK SFENFRFQPS LTILQVGSRP
DSSAYVKSKL KAAASSNIKS KLIKLDESIS QEDLVEVIER LNKDPKVHGI LVQLPLPKHI
DESVITNSVA TDKDVDGFDH YNVGQLSKRG GTPYFKPCTP NGIMELIKTT GIPLRGKTAV
VIGRSDIVGT PVATMLRNED CTVTVCHRYT QNLPEIVRQA DIVVAAVGIA EYVKADWVKD
GAIVIDVGIN YKDDPTAKRG RRLVGDVDYE EVAKKASFIT PVPGGVGPMT VAMLCSNVYD
AALIHAKKAH EHGFKPLELN IKDPVPSDIE ISRNQKPKKI TRVAQELGIL DAELEPYGHF
KAKVDPKSVI ERLDEQAEGS AQDKGNYVLV AGITPTPLGE GKSTTTMGLT QALGAHLGYN
AIANVRQPSM GPTFGVKGGA AGGGYAQVIP MDEFNMHLTG DIHAISAAQN LLCAAVDTRM
FHESTSKTTS GFYKRLVPVK KGKRSFTPSM LKRLEKLGIT KTNPDDLTAE EIEKFAVLNI
DPDSITIKRV VDCNDRFVRE ITIGEGKNEA SKYPPRKTGM DITVASELMA ILALSNSLKD
LRQRVGKLVV GTQRKTGEAI TAEDIGCAGA ITALLKDAIK PNLMQSLEGT PVFVHAGPFA
NISIGASSVI ADKLALKLTS PSNPINNGET GFVVTEAGFD FTMGGERFFN IKCRASGLKP
DAVVLVATSR ALKLHGGATD VKPGQPLPAE YVNENLEYLE KGCANLAKQI ANIKQYNVPV
VVAINQFETD TDAEIKLIQS LALKAGADFA VPSNHWAKGG AGAVELASSV VKAVKLAPLE
QQKYLYDVND TVENKLLAIT TKMYGASGIE LSPLAKKQIE TYTKQGYDKL PICIAKTQYS
LSHDPSLKGV PTEFTVPIRE VRCSAGAGYL YALAAEIMTI PGLPTHAGFM NVEVNDEGEI
EGLF
//
