MTHFS_MOUSE
ID MTHFS_MOUSE Reviewed; 203 AA.
AC Q9D110; B2KF82;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=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 Name=Mthfs;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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; AK004092; BAB23165.1; -; mRNA.
DR EMBL; AC135634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT030686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23394.1; -.
DR RefSeq; NP_081105.1; NM_026829.2.
DR AlphaFoldDB; Q9D110; -.
DR SMR; Q9D110; -.
DR BioGRID; 223657; 1.
DR STRING; 10090.ENSMUSP00000082354; -.
DR iPTMnet; Q9D110; -.
DR PhosphoSitePlus; Q9D110; -.
DR EPD; Q9D110; -.
DR MaxQB; Q9D110; -.
DR PaxDb; Q9D110; -.
DR PeptideAtlas; Q9D110; -.
DR PRIDE; Q9D110; -.
DR DNASU; 107885; -.
DR Ensembl; ENSMUST00000085256; ENSMUSP00000082354; ENSMUSG00000066442.
DR GeneID; 107885; -.
DR KEGG; mmu:107885; -.
DR UCSC; uc009qzk.1; mouse.
DR CTD; 10588; -.
DR MGI; MGI:1340032; Mthfs.
DR VEuPathDB; HostDB:ENSMUSG00000066442; -.
DR eggNOG; KOG3093; Eukaryota.
DR GeneTree; ENSGT00390000017791; -.
DR HOGENOM; CLU_066245_2_1_1; -.
DR InParanoid; Q9D110; -.
DR OMA; MPLVGFD; -.
DR OrthoDB; 1425233at2759; -.
DR PhylomeDB; Q9D110; -.
DR TreeFam; TF313668; -.
DR BRENDA; 6.3.3.2; 3474.
DR Reactome; R-MMU-196757; Metabolism of folate and pterines.
DR BioGRID-ORCS; 107885; 2 hits in 40 CRISPR screens.
DR ChiTaRS; Mthfs; mouse.
DR PRO; PR:Q9D110; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D110; protein.
DR Bgee; ENSMUSG00000066442; Expressed in granulocyte and 91 other tissues.
DR ExpressionAtlas; Q9D110; baseline and differential.
DR Genevisible; Q9D110; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0005542; F:folic acid binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032392; P:DNA geometric change; ISO:MGI.
DR GO; GO:0006353; P:DNA-templated transcription, termination; ISO:MGI.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0006393; P:termination of mitochondrial transcription; ISO:MGI.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Folate-binding; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49914"
FT CHAIN 2..203
FT /note="5-formyltetrahydrofolate cyclo-ligase"
FT /id="PRO_0000200276"
FT BINDING 10..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 145..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 148..152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P49914"
SQ SEQUENCE 203 AA; 23202 MW; 4C20DC7416CA5304 CRC64;
MAAVTVNSAK RGLRAELKQR LRALSAEERL RQSLLLTQKV IAHNQYQNSK RISIFLSMQD
EVETEVIIKD IFKQGKICFI PRYQFQSNHM DMVRLTSSEE IALLPKTSWN IHQPGEGDVR
EEALSTGGLD LIFLPGLGFD KDGNRLGRGK GYYDTYLKRC VQHQEVKPYT MALAFKEQIC
PQIPVDEHDM KVDEVLYEDS PAS
