ID   MTHFS_CAEEL             Reviewed;         206 AA.
AC   Q9XWE6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Probable 5-formyltetrahydrofolate cyclo-ligase;
DE            EC=6.3.3.2;
DE   AltName: Full=5,10-methenyl-tetrahydrofolate synthetase;
DE            Short=MTHFS;
DE            Short=Methenyl-THF synthetase;
GN   ORFNames=Y106G6E.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Contributes to tetrahydrofolate metabolism. Helps regulate
CC       carbon flow through the folate-dependent one-carbon metabolic network
CC       that supplies carbon for the biosynthesis of purines, thymidine and
CC       amino acids. Catalyzes the irreversible conversion of 5-
CC       formyltetrahydrofolate (5-CHO-H(4)PteGlu) to yield 5,10-
CC       methenyltetrahydrofolate (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = 5,10-
CC         methenyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:10488,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57455,
CC         ChEBI:CHEBI:57457, ChEBI:CHEBI:456216; EC=6.3.3.2;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC       family. {ECO:0000305}.
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DR   EMBL; AL032656; CAA21728.1; -; Genomic_DNA.
DR   PIR; T26418; T26418.
DR   RefSeq; NP_492692.1; NM_060291.5.
DR   AlphaFoldDB; Q9XWE6; -.
DR   SMR; Q9XWE6; -.
DR   BioGRID; 55484; 7.
DR   STRING; 6239.Y106G6E.4; -.
DR   EPD; Q9XWE6; -.
DR   PaxDb; Q9XWE6; -.
DR   PeptideAtlas; Q9XWE6; -.
DR   EnsemblMetazoa; Y106G6E.4.1; Y106G6E.4.1; WBGene00013708.
DR   GeneID; 190922; -.
DR   KEGG; cel:CELE_Y106G6E.4; -.
DR   UCSC; Y106G6E.4; c. elegans.
DR   CTD; 190922; -.
DR   WormBase; Y106G6E.4; CE20408; WBGene00013708; -.
DR   eggNOG; KOG3093; Eukaryota.
DR   GeneTree; ENSGT00390000017791; -.
DR   HOGENOM; CLU_066245_2_1_1; -.
DR   InParanoid; Q9XWE6; -.
DR   OMA; MPLVGFD; -.
DR   OrthoDB; 1425233at2759; -.
DR   PhylomeDB; Q9XWE6; -.
DR   Reactome; R-CEL-196757; Metabolism of folate and pterines.
DR   PRO; PR:Q9XWE6; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00013708; Expressed in embryo and 4 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR   Gene3D; 3.40.50.10420; -; 1.
DR   InterPro; IPR002698; FTHF_cligase.
DR   InterPro; IPR024185; FTHF_cligase-like_sf.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR23407:SF1; PTHR23407:SF1; 1.
DR   Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR   PIRSF; PIRSF006806; FTHF_cligase; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR02727; MTHFS_bact; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..206
FT                   /note="Probable 5-formyltetrahydrofolate cyclo-ligase"
FT                   /id="PRO_0000200278"
FT   BINDING         8..12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143..151
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         146..150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   206 AA;  23561 MW;  CAA2EF7A31F13039 CRC64;
     MSAIKEVKSE LRQFMKTLLG KISKEETQRQ TEAVFEKIIE SKWFQESKRL SVYVSTSGEI
     QTDSIIQKAL EMGKEVFIPQ FTKGSTAMDM VRVPDQTAFD NLPSTLWGIR QPEPKWKWQS
     YHETGPLDLI LAPGVAFSPY GLRCGHGKGY YDRFFSTHHK HFPENSPKKI GLALREQIIG
     TIPISETDVE LDEVIYEGET IIFDTI