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Protein

Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial

Gene

Mthfd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH.
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.

Cofactori

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

Magnesium, NAD

Enzyme and pathway databases

BRENDAi1.5.1.15. 3474.
SABIO-RKP18155.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
Including the following 2 domains:
NAD-dependent methylenetetrahydrofolate dehydrogenase (EC:1.5.1.15)
Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
Gene namesi
Name:Mthfd2
Synonyms:Nmdmc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1338850. Mthfd2.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535Mitochondrion1 PublicationAdd
BLAST
Chaini36 – 350315Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrialPRO_0000034050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP18155.
MaxQBiP18155.
PaxDbiP18155.
PRIDEiP18155.

PTM databases

PhosphoSiteiP18155.

Expressioni

Gene expression databases

BgeeiP18155.
ExpressionAtlasiP18155. baseline and differential.
GenevisibleiP18155. MM.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000005810.

Structurei

3D structure databases

ProteinModelPortaliP18155.
SMRiP18155. Positions 37-336.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0089. Eukaryota.
COG0190. LUCA.
GeneTreeiENSGT00840000129764.
HOGENOMiHOG000218242.
HOVERGENiHBG006411.
InParanoidiP18155.
KOiK13403.
OMAiCLDQSTM.
OrthoDBiEOG7CG70C.
PhylomeDBiP18155.
TreeFamiTF323998.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01576. THF_DHG_CYH.
InterProiIPR016040. 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]
PfamiPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00766. 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.

P18155-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVSLLSAL AVRLLRPTHG CHPRLQPFHL AAVRNEAVVI SGRKLAQQIK
60 70 80 90 100
QEVQQEVEEW VASGNKRPHL SVILVGDNPA SHSYVLNKTR AAAEVGINSE
110 120 130 140 150
TIVKPASVSE EELLNSIRKL NNDENVDGLL VQLPLPEHID ERKVCNAVSP
160 170 180 190 200
DKDVDGFHVI NVGRMCLDQY SMLPATPWGV WEIIKRTGIP TLGKNVVVAG
210 220 230 240 250
RSKNVGMPIA MLLHTDGAHE RPGGDATVTI SHRYTPKEQL KKHTILADIV
260 270 280 290 300
ISAAGIPNLI TADMIKEGAA VIDVGINRVQ DPVTAKPKLV GDVDFEGVKK
310 320 330 340 350
KAGYITPVPG GVGPMTVAML MKNTIIAAKK VLRPEELEVF KSKQRGVATN
Length:350
Mass (Da):37,863
Last modified:November 1, 1990 - v1
Checksum:i896AD40D9154E9D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04627 mRNA. Translation: AAA39827.1.
M63445
, 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.
CCDSiCCDS20277.1.
PIRiA33267.
RefSeqiNP_032664.1. NM_008638.2.
UniGeneiMm.443.
Mm.475021.

Genome annotation databases

EnsembliENSMUST00000005810; ENSMUSP00000005810; ENSMUSG00000005667.
GeneIDi17768.
KEGGimmu:17768.
UCSCiuc009cne.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04627 mRNA. Translation: AAA39827.1.
M63445
, 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.
CCDSiCCDS20277.1.
PIRiA33267.
RefSeqiNP_032664.1. NM_008638.2.
UniGeneiMm.443.
Mm.475021.

3D structure databases

ProteinModelPortaliP18155.
SMRiP18155. Positions 37-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000005810.

PTM databases

PhosphoSiteiP18155.

Proteomic databases

EPDiP18155.
MaxQBiP18155.
PaxDbiP18155.
PRIDEiP18155.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005810; ENSMUSP00000005810; ENSMUSG00000005667.
GeneIDi17768.
KEGGimmu:17768.
UCSCiuc009cne.2. mouse.

Organism-specific databases

CTDi10797.
MGIiMGI:1338850. Mthfd2.

Phylogenomic databases

eggNOGiKOG0089. Eukaryota.
COG0190. LUCA.
GeneTreeiENSGT00840000129764.
HOGENOMiHOG000218242.
HOVERGENiHBG006411.
InParanoidiP18155.
KOiK13403.
OMAiCLDQSTM.
OrthoDBiEOG7CG70C.
PhylomeDBiP18155.
TreeFamiTF323998.

Enzyme and pathway databases

BRENDAi1.5.1.15. 3474.
SABIO-RKP18155.

Miscellaneous databases

ChiTaRSiMthfd2. mouse.
NextBioi292477.
PROiP18155.
SOURCEiSearch...

Gene expression databases

BgeeiP18155.
ExpressionAtlasiP18155. baseline and differential.
GenevisibleiP18155. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01576. THF_DHG_CYH.
InterProiIPR016040. 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]
PfamiPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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: 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMTDC_MOUSE
AccessioniPrimary (citable) accession number: P18155
Secondary accession number(s): Q3TMN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 11, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.