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Q922D8

- C1TC_MOUSE

UniProt

Q922D8 - C1TC_MOUSE

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Protein
C-1-tetrahydrofolate synthase, cytoplasmic
Gene
Mthfd1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.UniRule annotation
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.UniRule annotation
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei197 – 1971NADP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi172 – 1743NADP By similarity
Nucleotide bindingi380 – 3878ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. formate-tetrahydrofolate ligase activity Source: RefGenome
  3. methenyltetrahydrofolate cyclohydrolase activity Source: RefGenome
  4. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: RefGenome
Complete GO annotation...

GO - Biological processi

  1. folic acid-containing compound biosynthetic process Source: InterPro
  2. histidine biosynthetic process Source: UniProtKB-KW
  3. methionine biosynthetic process Source: UniProtKB-KW
  4. one-carbon metabolic process Source: RefGenome
  5. purine nucleotide biosynthetic process Source: UniProtKB-KW
  6. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis, Methionine biosynthesis, One-carbon metabolism, Purine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_220137. Metabolism of folate and pterines.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
C-1-tetrahydrofolate synthase, cytoplasmic
Short name:
C1-THF synthase
Cleaved into the following chain:
Including the following 3 domains:
Methylenetetrahydrofolate dehydrogenase (EC:1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
Formyltetrahydrofolate synthetase (EC:6.3.4.3)
Gene namesi
Name:Mthfd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1342005. Mthfd1.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytosol Source: RefGenome
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Knockout mice have revealed Mthfd1l as a monofunctional enzyme having only formyltetrahydrofolate synthetase activity and lacking methenyl-THF dehydrogenase and cyclohydrolase activities.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 935935C-1-tetrahydrofolate synthase, cytoplasmicUniRule annotation
PRO_0000199322Add
BLAST
Initiator methioninei1 – 11Removed; alternate By similarity
Chaini2 – 935934C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processedUniRule annotation
PRO_0000423281Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ922D8.
PaxDbiQ922D8.
PRIDEiQ922D8.

2D gel databases

REPRODUCTION-2DPAGEQ922D8.

PTM databases

PhosphoSiteiQ922D8.

Expressioni

Gene expression databases

ArrayExpressiQ922D8.
BgeeiQ922D8.
GenevestigatoriQ922D8.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi223871. 1 interaction.
IntActiQ922D8. 5 interactions.
MINTiMINT-1856310.

Structurei

3D structure databases

ProteinModelPortaliQ922D8.
SMRiQ922D8. Positions 2-296, 316-935.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 305305Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseUniRule annotation
Add
BLAST
Regioni52 – 565Substrate binding By similarity
Regioni99 – 1013Substrate binding By similarity
Regioni272 – 2765Substrate binding By similarity
Regioni306 – 935630Formyltetrahydrofolate synthetaseUniRule annotation
Add
BLAST

Domaini

This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity.UniRule annotation

Sequence similaritiesi

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.

Phylogenomic databases

eggNOGiCOG0190.
GeneTreeiENSGT00750000117401.
HOVERGENiHBG004916.
InParanoidiQ8R013.
KOiK00288.
OMAiKWNISYT.
OrthoDBiEOG76T9QN.
TreeFamiTF300623.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPiMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProiIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q922D8-1 [UniParc]FASTAAdd to Basket

« Hide

MAPAGILNGK LVSAQIRDRL KNQVTRMQEQ VPGFTPGLAI LQVGDRDDSN    50
LYINVKLKAA EEIGIKATHI KLPRTSTESE VLKYVISLNE DASVHGFIVQ 100
LPLDSENSIN TEAVINAIAP EKDVDGLTSV SAGKLARGDL NDCFIPCTPK 150
GCLELIKEAG VQIAGRHAVV VGRSKIVGAP MHDLLLWNNA TVTTCHSKTA 200
NLDKEVNKGD ILVVATGQPE MVKGEWIKPG AVVIDCGINY VPDDTKPNGR 250
KVVGDVAYDE AKERASFITP VPGGVGPMTV AMLMQSTVES AQRFLQKFKP 300
GKWTIQYNKL NLKTPVPSDI AISRSCKPKL IGNLAREIGL LTEEVELYGE 350
TKAKVLLSAL DRLKHQPDGK YVVVTGITPT PLGEGKSTTT IGLVQALGAH 400
LRQNVFACVR QPSQGPTFGI KGGAAGGGYS QVIPMEEFNL HLTGDIHAIT 450
AANNLVAAAI DARIFHELTQ TDKALFNRLV PSVNGIRKFS DIQIRRLRRL 500
GIEKTDPTTL TDDEINRFAR LDIDPETITW QRVLDTNDRF LRKITIGQSP 550
TEKGHTRTAQ FDISVASEIM AVLALTSSLE DMRERLGRMV VASSKKGEPI 600
SCEDLGVSGA LTVLMKDAIK PNLMQTLEGT PVFVHAGPFA NIAHGNSSII 650
ADRIALKLVG PEGFVVTEAG FGADIGMEKF FNIKCRYSGL QPHVVVLVAT 700
VRALKMHGGG PTVTAGLPLP KAYTEEDLDL VEKGFSNLRK QIENARMFGV 750
PVVVAVNVFK TDTDAELDLV SRLSREHGAF DAVKCTHWAE GGQGALALAQ 800
AVQRASQAPS SFQLLYDLKL SIEDKIRIIA QRIYGADDIE LLPEAQNKAE 850
IYTKQGFGNL PICMAKTHLS LSHNPEQKGV PTGFVLPIRD IRASVGAGFL 900
YPLVGTMSTM PGLPTRPCFY DIDLDPETEQ VNGLF 935
Length:935
Mass (Da):101,200
Last modified:July 27, 2011 - v4
Checksum:i0EB92D58C78DDEB5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti365 – 3651H → Y in AAH08523. 1 Publication
Sequence conflicti610 – 6101A → T in AAH08523. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF364579 mRNA. Translation: AAL99692.1.
AF364591
, AF364580, AF364581, AF364582, AF364583, AF364584, AF364585, AF364586, AF364587, AF364588, AF364589, AF364590 Genomic DNA. Translation: AAL99693.1.
AK088700 mRNA. Translation: BAC40513.1.
BC008523 mRNA. Translation: AAH08523.1.
CCDSiCCDS25990.1.
RefSeqiNP_620084.2. NM_138745.2.
UniGeneiMm.29584.

Genome annotation databases

EnsembliENSMUST00000021443; ENSMUSP00000021443; ENSMUSG00000021048.
GeneIDi108156.
KEGGimmu:108156.
UCSCiuc007nxz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF364579 mRNA. Translation: AAL99692.1 .
AF364591
, AF364580 , AF364581 , AF364582 , AF364583 , AF364584 , AF364585 , AF364586 , AF364587 , AF364588 , AF364589 , AF364590 Genomic DNA. Translation: AAL99693.1 .
AK088700 mRNA. Translation: BAC40513.1 .
BC008523 mRNA. Translation: AAH08523.1 .
CCDSi CCDS25990.1.
RefSeqi NP_620084.2. NM_138745.2.
UniGenei Mm.29584.

3D structure databases

ProteinModelPortali Q922D8.
SMRi Q922D8. Positions 2-296, 316-935.
ModBasei Search...

Protein-protein interaction databases

BioGridi 223871. 1 interaction.
IntActi Q922D8. 5 interactions.
MINTi MINT-1856310.

Chemistry

ChEMBLi CHEMBL3137.

PTM databases

PhosphoSitei Q922D8.

2D gel databases

REPRODUCTION-2DPAGE Q922D8.

Proteomic databases

MaxQBi Q922D8.
PaxDbi Q922D8.
PRIDEi Q922D8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021443 ; ENSMUSP00000021443 ; ENSMUSG00000021048 .
GeneIDi 108156.
KEGGi mmu:108156.
UCSCi uc007nxz.2. mouse.

Organism-specific databases

CTDi 4522.
MGIi MGI:1342005. Mthfd1.

Phylogenomic databases

eggNOGi COG0190.
GeneTreei ENSGT00750000117401.
HOVERGENi HBG004916.
InParanoidi Q8R013.
KOi K00288.
OMAi KWNISYT.
OrthoDBi EOG76T9QN.
TreeFami TF300623.

Enzyme and pathway databases

UniPathwayi UPA00193 .
Reactomei REACT_220137. Metabolism of folate and pterines.

Miscellaneous databases

ChiTaRSi MTHFD1. mouse.
NextBioi 360186.
PROi Q922D8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q922D8.
Bgeei Q922D8.
Genevestigatori Q922D8.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPi MF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProi IPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view ]
Pfami PF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view ]
PRINTSi PR00085. THFDHDRGNASE.
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase derived from a trifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase-synthetase."
    Patel H., Christensen K.E., Mejia N., MacKenzie R.E.
    Arch. Biochem. Biophys. 403:145-148(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/SvJ.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 27-56; 59-66; 75-83; 123-134; 138-173; 176-198; 205-223; 251-262; 314-324; 330-352; 355-362; 371-402; 464-473; 488-495; 505-517; 521-532; 543-553; 658-679; 687-702; 706-733; 747-772; 776-784; 805-819; 833-848 AND 855-889, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "Disruption of the mthfd1 gene reveals a monofunctional 10-formyltetrahydrofolate synthetase in mammalian mitochondria."
    Christensen K.E., Patel H., Kuzmanov U., Mejia N.R., MacKenzie R.E.
    J. Biol. Chem. 280:7597-7602(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiC1TC_MOUSE
AccessioniPrimary (citable) accession number: Q922D8
Secondary accession number(s): Q8R013
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 109 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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