ID H2U4F9_TAKRU Unreviewed; 934 AA.
AC H2U4F9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic {ECO:0000256|ARBA:ARBA00017592};
DE EC=1.5.1.5 {ECO:0000256|ARBA:ARBA00012859};
DE EC=3.5.4.9 {ECO:0000256|ARBA:ARBA00012776};
DE EC=6.3.4.3 {ECO:0000256|ARBA:ARBA00012295};
GN Name=mthfd1 {ECO:0000313|Ensembl:ENSTRUP00000057293.1};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000057293.1, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000057293.1, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000057293.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:195366; EC=3.5.4.9;
CC Evidence={ECO:0000256|ARBA:ARBA00036357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10-
CC formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216;
CC EC=6.3.4.3; Evidence={ECO:0000256|ARBA:ARBA00036012};
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 RefSeq; XP_003962475.1; XM_003962426.2.
DR RefSeq; XP_011614609.1; XM_011616307.1.
DR AlphaFoldDB; H2U4F9; -.
DR STRING; 31033.ENSTRUP00000057293; -.
DR Ensembl; ENSTRUT00000051379.2; ENSTRUP00000057293.1; ENSTRUG00000012569.3.
DR GeneID; 101079275; -.
DR KEGG; tru:101079275; -.
DR CTD; 260441; -.
DR eggNOG; KOG4230; Eukaryota.
DR GeneTree; ENSGT00940000154746; -.
DR HOGENOM; CLU_003601_1_1_1; -.
DR InParanoid; H2U4F9; -.
DR OMA; QPIMFRR; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000005226; Chromosome 2.
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:SF1; 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:UP000005226}.
FT DOMAIN 6..124
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 128..292
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 934 AA; 100360 MW; 89547EB7B4AF3831 CRC64;
MSAQIISGKE VSAQVRECLK KDVEQMKLKD PNFSPGLVVL QVGDRDDSNL YISMKLKAAK
EIGINATHMR LPKTATEDEV LHSIKEVNEN SSVHGLIVQL PLDSVHKIDT EKVTNAVAPE
KDVDGLTSIN AGKLSRGDLG DCFIPCTPNG CMELIKQTGV SVAGKRAVVI GRSKIVGAPM
HDLLLWSHAT VTTCHSKTAD LPGEVGKADI LVVGIGKAEM VKGEWIKKGA VVIDCGINHI
PDASRPSGKR VVGDVHYASA KEQAGFITPV PGGVGPMTVA MLMANTVLSA KRFLESHQPG
KWNISYSNLN LQRPVPSDIV ISRSCVPKPI DHLAKEVGLL SDEVELFGTT KAKVRLNIVQ
RLQAQPDGKY VVVTGITPTP LGEGKSTTTI GLVQAMGAHM KLNVFACVRQ PSQGPTFGIK
GGAAGGGYSQ VIPMEEFNLH LTGDIHAITA ANNLVAAAID ARMFHESTQS DKALYNRLVP
LSGGERKFSP IQINRLKKLG IEKTDPSSLT EEEVTRFSRL DIDPSSVTWQ RVLDTNDRFL
RKITIGQSPT EKGYTREAQF DITVASEIMA VLALTTSLQD MRQRLAKMVV ATSRSGQPIT
TEDLGVSGAL TVLMKDAIKP NLMQTLEGNP VFVHAGPFAN IAHGNSSILA DKIALKLVGP
EGYVVTEAGF GADIGMEKFF NIKCRYSGLR PHVVVLVATV RALKMHGGGP TVTAGMPLPK
EYIDENLELL EKGCSNMKKQ IENAQHFGVP VVVAVNAFKT DTEAELDLVC SVAKAAGAFD
AVRCTHWAEG GAGAVALGQA VQRASEAPSS FKFLYDLELP IADKIRTIAR KIYGADDIEL
LPEAQLKVEL YTKQGFGNLP VCMAKTHLSL SHEADKKGVP TGFVLPIRDI RASTGAGFLF
PLVGTMPTIP GLPTRPCFYD IDLDPETEQV NGLF
//
