ID R9AGK6_WALI9 Unreviewed; 952 AA.
AC R9AGK6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=C-1-tetrahydrofolate synthase, cytoplasmic {ECO:0000313|EMBL:EOQ99195.1};
GN ORFNames=J056_002521 {ECO:0000313|EMBL:EOQ99195.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOQ99195.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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; KE007244; EOQ99195.1; -; Genomic_DNA.
DR RefSeq; XP_009270061.1; XM_009271786.1.
DR AlphaFoldDB; R9AGK6; -.
DR STRING; 1299270.R9AGK6; -.
DR GeneID; 20375473; -.
DR KEGG; wic:J056_002521; -.
DR eggNOG; KOG4230; Eukaryota.
DR HOGENOM; CLU_003601_1_0_1; -.
DR OMA; QPIMFRR; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000014064; 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; 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; 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:UP000014064}.
FT DOMAIN 6..119
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 122..288
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 952 AA; 101597 MW; 6607C9AD871328E6 CRC64;
MVGQKIDGTA IAKKLRGDLA TQTKTLPFNP HLVIIQHGAR PDSNSYIRMK RLAAEEAGFK
FTHIQIPDSD GVDKVLEHVR RCNQDDGVHG LLVQLPLANG GKDGERSVVE TISHDKDVDG
FHPLTAGALS SRLADPLFAP CTPAGVIKLL EESGVEIAGK FAVVLGRSDI VGTPAMNLLR
RKDATVVQVH SKTKNIPELV KQADIVVAAI GQPEFVKGEW IKEGAVVIDV GANFVPDATK
KSGQRMLGDV EYSKAIENAA HITPVPGGVG PMTVAMLMVN TFRAAERQAK LRGGRGRGVV
TPLPIHPLEQ VPSDIEIAMA QTPKPVSSLA QEIGVLDEEL ELYGQSKAKV ELSILDRLQH
RKDGKYVVVA GITPTPLGEG KSTTTVGLAQ ALGARLGRST FACVRQPSQG PTFGIKGGAA
GGGYSQIIPM DEFNLHLTGD IHAISAANNL LAAAIDARMF HESTQSAKAL YNRLTPAKKG
VRSFSPVMIK RLQKLGIDKT SPSDLNEEEV AKFAKLDIDP ETITWHRVTD TNDRYLRKIT
VGQAPTEKGI SRETGFDISV ASECMAVLAL ANDLPDMRRR LGDMVVASSK SGEPITADDI
GIGGALTVLM KDTIKPNLMQ TLEGTPVFVH AGPFANIAHG NSSILADRVA LKLAGTDEGE
PSSSGGYVIT EAGFGADIGM EKFFNIKCRV SGLVPDAVVL VATVRALKMH GGGPEVSPGK
PLDDIYTQEN LDTLAEGCKN LGKHIENGRK YGVKVIVAVN QFTTDTPAEL ELVKKLSYEA
GAHAAVASNH WALGGEGAID LAQSLIDTCE PKGSDGEVLP AQSNDDFKLL YDDNLTMEDK
ILTIVREMYG GEAIELSELA KSQVETYVKQ GYGNLPVCMA KSHLSLSHDP KLKGVPSGFT
VPIRSIKLSA GAGFVYALCG EMQTMPGLST RPGYYDIDLD MSGEKPRVVG LF
//
