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UniProtKB/Swiss-Prot entry P13995


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MTDC_HUMAN
Primary accession number P13995
Secondary accession numbers Q53G90 Q53GV5 Q53S36
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on September 19, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 90)
Name and origin of the protein
Protein name Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial [Precursor]
Synonyms None
Includes NAD-dependent methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.15)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Gene name
Name: MTHFD2
Synonyms: NMDMC
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-350.
DOI=10.1093/nar/17.21.8853; PubMed=2587219 [NCBI, ExPASy, EBI, Israel, Japan]
Peri K.G., Belanger C., Mackenzie R.E.;
"Nucleotide sequence of the human NAD-dependent methylene tetrahydrofolate dehydrogenase-cyclohydrolase.";
Nucleic Acids Res. 17:8853-8853(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver, and Thyroid;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, and Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X16396; CAA34431.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222826; BAD96546.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223041; BAD96761.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC073263; AAX93061.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001548; AAH01548.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017054; AAH17054.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S14902; DEHUMT.
RefSeq NP_006627.2; -.
UniGene Hs.469030
3D structure databases
PDB
1ZN4; Model; -; A/B=37-350.[ExPASy / RCSB / EBI]
PDBsum 1ZN4; -.
ModBase P13995.
PTM databases
PhosphoSite P13995; -.
Organism-specific databases
HGNC HGNC:7434; MTHFD2.
GenAtlas MTHFD2.
HPA CAB003684; -.
MIM 604887; gene. [NCBI / EBI]
PharmGKB PA31238; -.
GeneCards P13995.
Gene expression databases
CleanEx HS_MTHFD2; -.
GermOnline ENSG00000065911; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from sequence or structural similarity from UniProtKB).
GO:0000287; Molecular function: magnesium ion binding (inferred from direct assay from UniProtKB).
GO:0004477; Molecular function: methenyltetrahydrofolate cyclohydrolase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0004487; Molecular function: methylenetetrahydrofolate dehydrogenase (NAD+) activity (inferred from direct assay from UniProtKB).
GO:0004488; Molecular function: methylenetetrahydrofolate dehydrogenase (NADP+) activity (inferred from direct assay from UniProtKB).
GO:0042301; Molecular function: phosphate binding (inferred from direct assay from UniProtKB).
GO:0046653; Biological process: tetrahydrofolate metabolic process (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016040; NAD(P)-bd.
IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00763; THF_DHG_CYH; 1.
PF02882; THF_DHG_CYH_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00085; THFDHDRGNASE.
ProDom PD002300; THFDhg/Cyc_hydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00766; THF_DHG_CYH_1; 1.
PS00767; THF_DHG_CYH_2; 1.
BLOCKS P13995.
Genome annotation databases
Ensembl ENSG00000065911; Homo sapiens. [Contig view]
GeneID 10797; -.
NMPDR fig|9606.3.peg.18064; -.
Phylogenomic databases
HOGENOM P13995; -.
HOVERGEN P13995; -.
Other
DrugBank DB00157; NADH.
DB00116; Tetrahydrofolic acid.
LinkHub P13995; -.
SOURCE MTHFD2; Homo sapiens.
ProtoNet P13995.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Hydrolase; Magnesium; Mitochondrion; Multifunctional enzyme; NAD; One-carbon metabolism; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
TRANSIT   1    35  35     Mitochondrion (By similarity). 
CHAIN   36   350  315     Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial. PRO_0000034049
CONFLICT   75    75        V -> A (in Ref. 2; BAD96546). 
CONFLICT   95    95        V -> A (in Ref. 2; BAD96761). 
Sequence information
Length: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 37895 Da [This is the MW of the unprocessed precursor] CRC64: 4DBD263CF7BE28F4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAATSLMSAL AARLLQPAHS CSLRLRPFHL AAVRNEAVVI SGRKLAQQIK QEVRQEVEEW 

        70         80         90        100        110        120 
VASGNKRPHL SVILVGENPA SHSYVLNKTR AAAVVGINSE TIMKPASISE EELLNLINKL 

       130        140        150        160        170        180 
NNDDNVDGLL VQLPLPEHID ERRICNAVSP DKDVDGFHVI NVGRMCLDQY SMLPATPWGV 

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

       250        260        270        280        290        300 
KKHTILADIV ISAAGIPNLI TADMIKEGAA VIDVGINRVH DPVTAKPKLV GDVDFEGVRQ 

       310        320        330        340        350 
KAGYITPVPG GVGPMTVAML MKNTIIAAKK VLRLEEREVL KSKELGVATN 

P13995 in FASTA format

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