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Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase (EC 1.5.1.15); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)]

 MTDC_HUMAN              Reviewed;         350 AA.
P13995; Q53G90; Q53GV5; Q53S36; Q7Z650;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
19-SEP-2006, sequence version 2.
12-SEP-2018, entry version 196.
RecName: Full=Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial;
Includes:
RecName: Full=NAD-dependent methylenetetrahydrofolate dehydrogenase {ECO:0000303|PubMed:16100107};
EC=1.5.1.15;
Includes:
RecName: Full=Methenyltetrahydrofolate cyclohydrolase;
EC=3.5.4.9;
Flags: Precursor;
Name=MTHFD2; Synonyms=NMDMC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-350 (ISOFORM 1).
PubMed=2587219; DOI=10.1093/nar/17.21.8853;
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] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Cervix, and Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[10]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ASN-35, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[12]
3D-STRUCTURE MODELING OF 36-350 IN COMPLEX WITH NAD AND PHOSPHATE,
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF ASP-168; ARG-201; ASP-225 AND ARG-233.
PubMed=16100107; DOI=10.1074/jbc.M505210200;
Christensen K.E., Mirza I.A., Berghuis A.M., Mackenzie R.E.;
"Magnesium and phosphate ions enable NAD binding to
methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate
cyclohydrolase.";
J. Biol. Chem. 280:34316-34323(2005).
[13] {ECO:0000244|PDB:5TC4}
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 36-350 IN COMPLEX WITH
PHOSPHATE; NAD AND INHIBITOR, AND SUBUNIT.
PubMed=27899380; DOI=10.1158/0008-5472.CAN-16-1476;
Gustafsson R., Jemth A.S., Gustafsson N.M., Farnegardh K., Loseva O.,
Wiita E., Bonagas N., Dahllund L., Llona-Minguez S., Haggblad M.,
Henriksson M., Andersson Y., Homan E., Helleday T., Stenmark P.;
"Crystal structure of the emerging cancer target MTHFD2 in complex
with a substrate-based inhibitor.";
Cancer Res. 77:937-948(2017).
-!- FUNCTION: Although its dehydrogenase activity is NAD-specific, it
can also utilize NADP at a reduced efficiency.
{ECO:0000269|PubMed:16100107}.
-!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NAD(+) =
5,10-methenyltetrahydrofolate + NADH.
{ECO:0000269|PubMed:16100107}.
-!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10-
formyltetrahydrofolate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=202 uM for NAD {ECO:0000269|PubMed:16100107};
KM=352 uM for NADP {ECO:0000269|PubMed:16100107};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27899380}.
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P13995-1; Sequence=Displayed;
Name=2;
IsoId=P13995-2; Sequence=VSP_056188;
-!- DEVELOPMENTAL STAGE: Expressed only in developing normal tissues.
-!- 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.
-!- SIMILARITY: Belongs to the tetrahydrofolate
dehydrogenase/cyclohydrolase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAX93061.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAD96546.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAD96761.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA34431.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X16396; CAA34431.1; ALT_INIT; mRNA.
EMBL; AK300035; BAG61846.1; -; mRNA.
EMBL; AK222826; BAD96546.1; ALT_INIT; mRNA.
EMBL; AK223041; BAD96761.1; ALT_INIT; mRNA.
EMBL; AC073263; AAX93061.1; ALT_INIT; Genomic_DNA.
EMBL; CH471053; EAW99671.1; -; Genomic_DNA.
EMBL; CH471053; EAW99672.1; -; Genomic_DNA.
EMBL; BC001548; AAH01548.2; -; mRNA.
EMBL; BC015062; AAH15062.1; -; mRNA.
EMBL; BC017054; AAH17054.2; -; mRNA.
CCDS; CCDS1935.2; -. [P13995-1]
PIR; S14902; DEHUMT.
RefSeq; NP_006627.2; NM_006636.3. [P13995-1]
RefSeq; XP_006711987.1; XM_006711924.2. [P13995-2]
UniGene; Hs.469030; -.
PDB; 1ZN4; Model; -; A/B=37-350.
PDB; 5TC4; X-ray; 1.89 A; A=36-350.
PDBsum; 1ZN4; -.
PDBsum; 5TC4; -.
ProteinModelPortal; P13995; -.
SMR; P13995; -.
BioGrid; 116011; 30.
IntAct; P13995; 13.
MINT; P13995; -.
STRING; 9606.ENSP00000377617; -.
BindingDB; P13995; -.
ChEMBL; CHEMBL3621036; -.
DrugBank; DB00157; NADH.
DrugBank; DB00116; Tetrahydrofolic acid.
iPTMnet; P13995; -.
PhosphoSitePlus; P13995; -.
BioMuta; MTHFD2; -.
DMDM; 115311607; -.
EPD; P13995; -.
MaxQB; P13995; -.
PaxDb; P13995; -.
PeptideAtlas; P13995; -.
PRIDE; P13995; -.
ProteomicsDB; 53016; -.
DNASU; 10797; -.
Ensembl; ENST00000394053; ENSP00000377617; ENSG00000065911. [P13995-1]
GeneID; 10797; -.
KEGG; hsa:10797; -.
UCSC; uc002skk.4; human. [P13995-1]
CTD; 10797; -.
DisGeNET; 10797; -.
EuPathDB; HostDB:ENSG00000065911.11; -.
GeneCards; MTHFD2; -.
HGNC; HGNC:7434; MTHFD2.
HPA; CAB003684; -.
HPA; HPA049657; -.
MIM; 604887; gene.
neXtProt; NX_P13995; -.
OpenTargets; ENSG00000065911; -.
PharmGKB; PA31238; -.
eggNOG; KOG0089; Eukaryota.
eggNOG; COG0190; LUCA.
GeneTree; ENSGT00920000149057; -.
HOGENOM; HOG000218242; -.
HOVERGEN; HBG006411; -.
InParanoid; P13995; -.
KO; K13403; -.
OMA; AGKLCGD; -.
OrthoDB; EOG091G0VB7; -.
PhylomeDB; P13995; -.
TreeFam; TF323998; -.
BRENDA; 1.5.1.15; 2681.
Reactome; R-HSA-196757; Metabolism of folate and pterines.
SABIO-RK; P13995; -.
ChiTaRS; MTHFD2; human.
GeneWiki; MTHFD2; -.
GenomeRNAi; 10797; -.
PRO; PR:P13995; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000065911; Expressed in 228 organ(s), highest expression level in left coronary artery.
CleanEx; HS_MTHFD2; -.
ExpressionAtlas; P13995; baseline and differential.
Genevisible; P13995; HS.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; ISS:UniProtKB.
GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; IDA:UniProtKB.
GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IDA:UniProtKB.
GO; GO:0042301; F:phosphate ion binding; IDA:UniProtKB.
GO; GO:0046655; P:folic acid metabolic process; TAS:Reactome.
GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
GO; GO:0046653; P:tetrahydrofolate metabolic process; IDA:UniProtKB.
HAMAP; MF_01576; THF_DHG_CYH; 1.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR000672; THF_DH/CycHdrlase.
InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
InterPro; IPR020867; THF_DH/CycHdrlase_CS.
InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
PANTHER; PTHR10025; PTHR10025; 1.
Pfam; PF00763; THF_DHG_CYH; 1.
Pfam; PF02882; THF_DHG_CYH_C; 1.
PRINTS; PR00085; THFDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00766; THF_DHG_CYH_1; 1.
PROSITE; PS00767; THF_DHG_CYH_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Hydrolase; Isopeptide bond; Magnesium; Mitochondrion;
Multifunctional enzyme; NAD; NADP; One-carbon metabolism;
Oxidoreductase; Reference proteome; Transit peptide; Ubl conjugation.
TRANSIT 1 35 Mitochondrion.
{ECO:0000244|PubMed:25944712}.
CHAIN 36 350 Bifunctional methylenetetrahydrofolate
dehydrogenase/cyclohydrolase,
mitochondrial.
/FTId=PRO_0000034049.
NP_BIND 200 202 NAD. {ECO:0000269|PubMed:16100107,
ECO:0000269|PubMed:27899380}.
REGION 84 88 Substrate binding.
{ECO:0000269|PubMed:27899380}.
REGION 131 133 Substrate binding.
{ECO:0000269|PubMed:27899380}.
REGION 309 313 Substrate binding.
{ECO:0000269|PubMed:27899380}.
BINDING 233 233 NAD. {ECO:0000269|PubMed:16100107,
ECO:0000269|PubMed:27899380}.
MOD_RES 50 50 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 50 50 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 102 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_056188.
MUTAGEN 168 168 D->A: Significant loss of NAD and NADP-
dependent dehydrogenase specific
activity. {ECO:0000269|PubMed:16100107}.
MUTAGEN 168 168 D->E: Complete loss of NAD and NADP-
dependent dehydrogenase specific
activity. {ECO:0000269|PubMed:16100107}.
MUTAGEN 168 168 D->N: 80% decrease in NAD-dependent
dehydrogenase specific activity. 18%
decrease in NADP-dependent dehydrogenase
specific activity. Reduced affinity for
magnesium. {ECO:0000269|PubMed:16100107}.
MUTAGEN 168 168 D->S: 82% decrease in NAD-dependent
dehydrogenase specific activity. 65%
decrease in NADP-dependent dehydrogenase
specific activity. Reduced affinity for
magnesium. {ECO:0000269|PubMed:16100107}.
MUTAGEN 201 201 R->A,S,K: Complete loss of NAD and NADP-
dependent dehydrogenase specific
activity. {ECO:0000269|PubMed:16100107}.
MUTAGEN 225 225 D->A,S,E: Complete loss of NAD and NADP-
dependent dehydrogenase specific
activity. {ECO:0000269|PubMed:16100107}.
MUTAGEN 225 225 D->N: 84% decrease in NAD-dependent
dehydrogenase specific activity. 36%
increase in NADP-dependent dehydrogenase
specific activity. Reduced affinity for
magnesium. {ECO:0000269|PubMed:16100107}.
MUTAGEN 233 233 R->A: Significant loss of NAD and NADP-
dependent dehydrogenase specific
activity. {ECO:0000269|PubMed:16100107}.
MUTAGEN 233 233 R->K: 50% decrease in NAD and NADP-
dependent dehydrogenase specific
activity. Reduced affinity for magnesium.
{ECO:0000269|PubMed:16100107}.
MUTAGEN 233 233 R->S: Almost complete loss of NAD-
dependent dehydrogenase specific
activity. 50% decrease in NADP-dependent
dehydrogenase specific activity.
{ECO:0000269|PubMed:16100107}.
CONFLICT 75 75 V -> A (in Ref. 3; BAD96546).
{ECO:0000305}.
CONFLICT 95 95 V -> A (in Ref. 3; BAD96761).
{ECO:0000305}.
HELIX 42 62 {ECO:0000244|PDB:5TC4}.
STRAND 69 76 {ECO:0000244|PDB:5TC4}.
HELIX 79 95 {ECO:0000244|PDB:5TC4}.
STRAND 98 104 {ECO:0000244|PDB:5TC4}.
HELIX 110 122 {ECO:0000244|PDB:5TC4}.
STRAND 128 131 {ECO:0000244|PDB:5TC4}.
HELIX 141 147 {ECO:0000244|PDB:5TC4}.
HELIX 150 152 {ECO:0000244|PDB:5TC4}.
HELIX 159 166 {ECO:0000244|PDB:5TC4}.
HELIX 175 187 {ECO:0000244|PDB:5TC4}.
STRAND 195 199 {ECO:0000244|PDB:5TC4}.
TURN 203 205 {ECO:0000244|PDB:5TC4}.
HELIX 206 214 {ECO:0000244|PDB:5TC4}.
STRAND 219 221 {ECO:0000244|PDB:5TC4}.
STRAND 227 231 {ECO:0000244|PDB:5TC4}.
HELIX 237 244 {ECO:0000244|PDB:5TC4}.
STRAND 248 252 {ECO:0000244|PDB:5TC4}.
HELIX 262 264 {ECO:0000244|PDB:5TC4}.
STRAND 270 273 {ECO:0000244|PDB:5TC4}.
STRAND 277 279 {ECO:0000244|PDB:5TC4}.
STRAND 288 290 {ECO:0000244|PDB:5TC4}.
HELIX 295 298 {ECO:0000244|PDB:5TC4}.
TURN 299 301 {ECO:0000244|PDB:5TC4}.
STRAND 303 305 {ECO:0000244|PDB:5TC4}.
STRAND 308 311 {ECO:0000244|PDB:5TC4}.
HELIX 312 329 {ECO:0000244|PDB:5TC4}.
SEQUENCE 350 AA; 37895 MW; 4DBD263CF7BE28F4 CRC64;
MAATSLMSAL AARLLQPAHS CSLRLRPFHL AAVRNEAVVI SGRKLAQQIK QEVRQEVEEW
VASGNKRPHL SVILVGENPA SHSYVLNKTR AAAVVGINSE TIMKPASISE EELLNLINKL
NNDDNVDGLL VQLPLPEHID ERRICNAVSP DKDVDGFHVI NVGRMCLDQY SMLPATPWGV
WEIIKRTGIP TLGKNVVVAG RSKNVGMPIA MLLHTDGAHE RPGGDATVTI SHRYTPKEQL
KKHTILADIV ISAAGIPNLI TADMIKEGAA VIDVGINRVH DPVTAKPKLV GDVDFEGVRQ
KAGYITPVPG GVGPMTVAML MKNTIIAAKK VLRLEEREVL KSKELGVATN


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Catalog number Product name Quantity
CSB-EL015156HU Human Bifunctional methylenetetrahydrofolate dehydrogenase per cyclohydrolase, mitochondrial [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase(MTHFD2) ELISA kit 96T
30-142 MTHFD2 is a nuclear-encoded mitochondrial bifunctional enzyme with methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities. The enzyme functions as a homodimer a 0.1 mg
26-095 This protein is a nuclear-encoded mitochondrial bifunctional enzyme with methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities. The enzyme functions as a homod 0.05 mg
CSB-EL015156BO Bovine Bifunctional methylenetetrahydrofolate dehydrogenase_cyclohydrolase, mitochondrial [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase(MTHFD2) ELISA kit 96T
CSB-EL015156CH Chicken Bifunctional methylenetetrahydrofolate dehydrogenase_cyclohydrolase, mitochondrial [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase(MTHFD2) ELISA kit 96T
CSB-EL015156HU Human Bifunctional methylenetetrahydrofolate dehydrogenase_cyclohydrolase, mitochondrial [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase(MTHFD2) ELISA kit 96T
CSB-EL015156MO Mouse Bifunctional methylenetetrahydrofolate dehydrogenase_cyclohydrolase, mitochondrial [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase(MTHFD2) ELISA kit 96T
CSB-EL015156HU Human Bifunctional methylenetetrahydrofolate dehydrogenase_cyclohydrolase, mitochondrial [Includes NAD-dependent methylenetetrahydrofolate dehydrogenase(MTHFD2) ELISA kit SpeciesHuman 96T
CSB-EL015156MO Mouse Bifunctional methylenetetrahydrofolate dehydrogenase_cyclohydrolase, mitochondrial [Includes NAD-dependent methylenetetrahydrofolate dehydrogenase(MTHFD2) ELISA kit SpeciesMouse 96T
CSB-EL015156BO Bovine Bifunctional methylenetetrahydrofolate dehydrogenase_cyclohydrolase, mitochondrial [Includes NAD-dependent methylenetetrahydrofolate dehydrogenase(MTHFD2) ELISA kit SpeciesBovine 96T
CSB-EL015156CH Chicken Bifunctional methylenetetrahydrofolate dehydrogenase_cyclohydrolase, mitochondrial [Includes NAD-dependent methylenetetrahydrofolate dehydrogenase(MTHFD2) ELISA kit SpeciesChicken 96T
MTHFR MTHFD2 Gene methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase
201-20-3535 MTHFD2{methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase}rabbit.pAb 0.2ml
MTDC_HUMAN Human ELISA Kit FOR Bifunctional methylenetetrahydrofolate dehydrogenase per cyclohydrolase, mitochondrial 96T
201-20-3533 MTHFD1{methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase}rabbit.pAb 0.2ml
MTHFD2 MTHFD1 Gene methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase
MTDC_BOVIN ELISA Kit FOR Bifunctional methylenetetrahydrofolate dehydrogenase per cyclohydrolase, mitochondrial; organism: Bovine; gene name: MTHFD2 96T
MTDC_HUMAN ELISA Kit FOR Bifunctional methylenetetrahydrofolate dehydrogenase per cyclohydrolase, mitochondrial; organism: Human; gene name: MTHFD2 96T
CSB-EL015153RA Rat methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase (MTHFD1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL015156BO Bovine methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase (MTHFD2) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL015156HU Human methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase (MTHFD2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL015156CH Chicken methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase (MTHFD2) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL015156MO Mouse methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase (MTHFD2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
E1980h Mouse ELISA Kit FOR Probable bifunctional methylenetetrahydrofolate dehydrogenase per cyclohydrolase 2 96T
G1024 Probable bifunctional methylenetetrahydrofolate dehydrogenase cyclohydrolase 2 (MTHFD2L), Human, ELISA Kit 96T


 

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