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P18155 (MTDC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial

Including the following 2 domains:

  1. NAD-dependent methylenetetrahydrofolate dehydrogenase
    EC=1.5.1.15
  2. Methenyltetrahydrofolate cyclohydrolase
    EC=3.5.4.9
Gene names
Name:Mthfd2
Synonyms:Nmdmc
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH.

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.

Cofactor

Magnesium.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion.

Miscellaneous

This NAD-dependent bifunctional enzyme has very different kinetic properties than the larger NADP-dependent trifunctional enzyme and is unique in that it requires formation of an enzyme-magnesium complex to allow binding of NAD.

Sequence similarities

Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion Ref.1
Chain36 – 350315Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
PRO_0000034050

Amino acid modifications

Modified residue501N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P18155 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 896AD40D9154E9D7

FASTA35037,863
        10         20         30         40         50         60 
MASVSLLSAL AVRLLRPTHG CHPRLQPFHL AAVRNEAVVI SGRKLAQQIK QEVQQEVEEW 

        70         80         90        100        110        120 
VASGNKRPHL SVILVGDNPA SHSYVLNKTR AAAEVGINSE TIVKPASVSE EELLNSIRKL 

       130        140        150        160        170        180 
NNDENVDGLL VQLPLPEHID ERKVCNAVSP DKDVDGFHVI NVGRMCLDQY SMLPATPWGV 

       190        200        210        220        230        240 
WEIIKRTGIP TLGKNVVVAG RSKNVGMPIA MLLHTDGAHE RPGGDATVTI SHRYTPKEQL 

       250        260        270        280        290        300 
KKHTILADIV ISAAGIPNLI TADMIKEGAA VIDVGINRVQ DPVTAKPKLV GDVDFEGVKK 

       310        320        330        340        350 
KAGYITPVPG GVGPMTVAML MKNTIIAAKK VLRPEELEVF KSKQRGVATN

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of cDNA clones encoding the murine NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase."
Belanger C., Mackenzie R.E.
J. Biol. Chem. 264:4837-4843(1989) [PubMed: 2647744] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-55.
[2]"Structural organization of the murine gene encoding NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase."
Belanger C., Mackenzie R.E.
Gene 97:283-288(1991) [PubMed: 1999293] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Salivary gland.
[5]"Analysis of the promoter region of the gene encoding NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase."
Belanger C., Peri K.G., Mackenzie R.E.
Nucleic Acids Res. 19:4341-4345(1991) [PubMed: 1843253] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04627 mRNA. Translation: AAA39827.1.
M63445 expand/collapse EMBL AC list , M63415, M63439, M63440, M63441, M63442, M63443, M63444 Genomic DNA. Translation: AAA39828.1.
AK076019 mRNA. Translation: BAC36124.1.
AK159680 mRNA. Translation: BAE35283.1.
AK165840 mRNA. Translation: BAE38407.1.
BC019511 mRNA. Translation: AAH19511.1.
S52980 Genomic DNA. No translation available.
IPIIPI00109824.
PIRA33267.
RefSeqNP_032664.1. NM_008638.2.
UniGeneMm.443.
Mm.475021.

3D structure databases

ProteinModelPortalP18155.
SMRP18155. Positions 37-336.
ModBaseSearch...

Protein-protein interaction databases

STRINGP18155.

PTM databases

PhosphoSiteP18155.

Proteomic databases

PRIDEP18155.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005810; ENSMUSP00000005810; ENSMUSG00000005667.
GeneID17768.
KEGGmmu:17768.
NMPDRfig|10090.3.peg.14707.
UCSCuc009cne.2. mouse.

Organism-specific databases

CTD10797.
MGIMGI:1338850. Mthfd2.

Phylogenomic databases

eggNOGroNOG07067.
HOGENOMHBG328751.
HOVERGENHBG006411.
InParanoidP18155.
OMANQDERVD.
OrthoDBEOG4N5VZ4.
PhylomeDBP18155.

Enzyme and pathway databases

BRENDA1.5.1.15. 3474.

Gene expression databases

ArrayExpressP18155.
BgeeP18155.
GenevestigatorP18155.
GermOnlineENSMUSG00000005667. Mus musculus.

Family and domain databases

InterProIPR016040. NAD(P)-bd_dom.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK13403.
PfamPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSPR00085. THFDHDRGNASE.
PROSITEPS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio292477.
SOURCESearch...

Entry information

Entry nameMTDC_MOUSE
AccessionPrimary (citable) accession number: P18155
Secondary accession number(s): Q3TMN4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: December 14, 2011
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents