ID   A0A1G4IRA8_9SACH        Unreviewed;       944 AA.
AC   A0A1G4IRA8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=LAMI_0A08086g1_1 {ECO:0000313|EMBL:SCU79278.1};
GN   ORFNames=LAMI_0A08086G {ECO:0000313|EMBL:SCU79278.1};
OS   Lachancea mirantina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU79278.1, ECO:0000313|Proteomes:UP000191024};
RN   [1] {ECO:0000313|EMBL:SCU79278.1, ECO:0000313|Proteomes:UP000191024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 11717 {ECO:0000313|EMBL:SCU79278.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) 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}.
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DR   EMBL; LT598462; SCU79278.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4IRA8; -.
DR   STRING; 1230905.A0A1G4IRA8; -.
DR   OrthoDB; 651667at2759; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000191024; Chromosome a.
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; 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:SF8; 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   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191024}.
FT   DOMAIN          6..122
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          126..292
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   944 AA;  102323 MW;  803F5091F126DEC5 CRC64;
     MTATLIDGKA IAKEIREEIL RDIQQIRNEN SSFKPTLAIF QVSDRQDSST YVRMKRKAAE
     EAGIEVIFVH LPEDVEERSL IAQIEEMNQD RSVDGILVQL PLPKHIDEDK VTSAVMAQKD
     VDGFGPFNIG ELNKRNGKPY FHPCTPKGII ELLDRSGVQI AGSRAVVIGR SDIVGAPVAE
     LLKSRDATVT VLHSKSKDIP LYVSTADIIV VAIGRADFVK GEWFKGNKNA VVIDVGTNYV
     EDTSKKSGYR CVGDVEFDVA REHVELITPV PGGVGPMTVA MLMRNCLDAA RRSLQGDDKP
     AFAPLPLNLL KPVPSDFEIS RAQKPKEITQ VAYEAGILAS ELEPYGSTKA KVKLDILDRL
     KSRENGKYVL VTGITPTPLG EGKSTTTVGL AQALGAHLNK TVFANVRQPS MGPTFGIKGG
     AAGGGYSQVI PMDEFNLHVT GDIHAISMAN NLLAAAIDTR MFHETTQKDA ALYKRLVPTK
     RGIRKFTPTM LRRLKKLGIE KQDPNTLTPE EVTRFARLDI DPETITWRRV VDCNDRFLRG
     ITVGEAPTER GFTRKTGFDI SVASECMAVL ALANSLPDMR ERLGNIVVAA SKAGEPITCE
     DIGCAGAMTA LLKDAIKPNI MQTLEGTPVF VHAGPFANIS IGANSALADK MALKLAGVDK
     ALSPEQRREK QGYVVTEAGF DFTMGGERFL NIKCRSSGLV PDVVIIVATV RALKVHGGGP
     EVKAGAPLPS EYLNENVDLL RKGCANLAKH ISNAKAYNLP VLVAINRMSS DSDREHEVIR
     EESLKAGAVD AIVSNHWEEG GQGAIALAQG VVDACEATNQ FKFLYETKGV SVEDKIRTIA
     TEMYGAGDVE FLTEAQKKID LYTKQGFGDL PICIAKTQYS LSHDANLKGV PTGFTFPIRD
     VRASVGAGYL YALAAEIQTI PGLPTHCGFM NVEVNDDGEI DGMF
//