ID A0A367YKT7_9ASCO Unreviewed; 946 AA.
AC A0A367YKT7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=C-1-tetrahydrofolate synthase, mitochondrial {ECO:0000313|EMBL:RCK66350.1};
GN Name=MIS1_1 {ECO:0000313|EMBL:RCK66350.1};
GN ORFNames=Cantr_02046 {ECO:0000313|EMBL:RCK66350.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK66350.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK66350.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK66350.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RCK66350.1}.
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DR EMBL; QLNQ01000016; RCK66350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367YKT7; -.
DR STRING; 5486.A0A367YKT7; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000253472; Unassembled WGS sequence.
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; PS00722; FTHFS_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000253472}.
FT DOMAIN 6..122
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 126..293
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 946 AA; 101890 MW; 2BB4E1FF224D78CF CRC64;
MVAELIDGKA IALDLRTKIH DEIEQFQAKH LDFKPHLSII QVGDRPDSTT YVKMKLKAAE
EASIGCEIIK LPEDISEFEL LNKVEKLNNS LDVDGVLVQL PLPSHIDEVK VTNAVLADKD
VDGFGPFNVG ELAKKGGEPL FLPCTPKGIM YLLEKSGVDL EGKDAVVLGR SDIVGKPIAN
LLTKANANVT VVHSKTPLDK IQRYLGDADI VVAAIGQPAF VKGEWLKEGA VVIDVGTNFI
PDATKKSGQR MIGDVEFDVA KNKVALITPV PGGVGPMTVA CLLDNVVAAA KRHYEANNQT
PKFTNPLKLN LQKPVPSDFE ISRAQQPKRI TQVAEEAGIL DAELEPFGFY KAKVSLDILK
RLQHKQNGKY VLVTGITPTP LGEGKSTTTV GLAQALGAHL NKNVFANVRQ PSMGPTFGIK
GGAAGGGYSQ VIPMDEFNMH VTGDIHAITM ANNLLAAAID TRMFHENTQK DGPLYKRLVP
EKKGTRKFTS SMLRRLKKLG IDKTDPNELT PEEITQFARL DIDPETITWR RVVDCNDRFL
RGITVGQAPT EKGFTRATGF DITVASECMA ILALANSLED MRERLGRMVI GSSKAGVPIT
CEDIGCAGAL TALLKDAIKP NIMQTLEGTP VFVHAGPFAN ISIGASSILA DKMALKLAGT
SPDLTPEEKK EQEGYVVTEA GFDFTMGGER FINIKCRSSG LVPDVIVIVA TVRALKVHGG
GPEVKAGAPL APEYTQENVE LLRAGCSNLA KHIANAKSYG LPVVVAINKM SSDSDREHEV
IKEEALKAGA VDAIVSNHWE EGGKGAVDLA KGVMEAANAP ERDFHFLYGL EPSVEDKISA
IATEMYGAGE VEFLPEAQKK IDLYTKQGFG KLPVCIAKTQ YSLSHDASLK GVPTGFKFPI
RDVRASIGAG YLYALAAEIQ TIPGLPTHCG FMNVEVNEDG EIDGLF
//
