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A6H5Y3

- METH_MOUSE

UniProt

A6H5Y3 - METH_MOUSE

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Protein
Methionine synthase
Gene
Mtr
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate By similarity.

Catalytic activityi

5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.

Cofactori

Methylcobalamin (MeCBL) By similarity.
Binds 1 zinc ion per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi248 – 2481Zinc By similarity
Metal bindingi311 – 3111Zinc By similarity
Metal bindingi312 – 3121Zinc By similarity
Metal bindingi773 – 7731Cobalt (cobalamin axial ligand) By similarity
Binding sitei818 – 8181Cobalamin By similarity
Binding sitei962 – 9621S-adenosyl-L-methionine By similarity
Binding sitei1160 – 11601S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei1164 – 11641Cobalamin; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
  2. cobalamin binding Source: UniProtKB-KW
  3. methionine synthase activity Source: MGI
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. methionine biosynthetic process Source: MGI
  2. pteridine-containing compound metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

ReactomeiREACT_189091. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
REACT_189092. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_202492. Sulfur amino acid metabolism.
UniPathwayiUPA00051; UER00081.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine synthase (EC:2.1.1.13)
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Vitamin-B12 dependent methionine synthase
Short name:
MS
Gene namesi
Name:Mtr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:894292. Mtr.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12531253Methionine synthase
PRO_0000312901Add
BLAST

Proteomic databases

MaxQBiA6H5Y3.
PaxDbiA6H5Y3.
PRIDEiA6H5Y3.

PTM databases

PhosphoSiteiA6H5Y3.

Expressioni

Gene expression databases

BgeeiA6H5Y3.
GenevestigatoriA6H5Y3.

Structurei

3D structure databases

ProteinModelPortaliA6H5Y3.
SMRiA6H5Y3. Positions 4-639, 653-908, 914-1252.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 326321Hcy-binding
Add
BLAST
Domaini359 – 620262Pterin-binding
Add
BLAST
Domaini650 – 74798B12-binding N-terminal
Add
BLAST
Domaini760 – 895136B12-binding
Add
BLAST
Domaini911 – 1253343AdoMet activation
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni848 – 8492Cobalamin-binding By similarity
Regioni1215 – 12162S-adenosyl-L-methionine binding By similarity

Domaini

Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin By similarity.

Sequence similaritiesi

Contains 1 B12-binding domain.
Contains 1 Hcy-binding domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1410.
GeneTreeiENSGT00420000029824.
HOGENOMiHOG000251409.
HOVERGENiHBG006347.
InParanoidiA6H5Y3.
KOiK00548.
OMAiLTEHYAM.
OrthoDBiEOG7TF786.
PhylomeDBiA6H5Y3.
TreeFamiTF312829.

Family and domain databases

Gene3Di1.10.1240.10. 1 hit.
3.10.196.10. 1 hit.
3.20.20.20. 1 hit.
3.20.20.330. 1 hit.
3.40.50.280. 1 hit.
InterProiIPR003759. Cbl-bd_cap.
IPR006158. Cobalamin-bd.
IPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
IPR003726. S_MeTrfase.
IPR004223. VitB12-dep_Met_synth_activ_dom.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
PF02607. B12-binding_2. 1 hit.
PF02965. Met_synt_B12. 1 hit.
PF00809. Pterin_bind. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFiPIRSF000381. MetH. 1 hit.
SMARTiSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMiSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsiTIGR02082. metH. 1 hit.
PROSITEiPS50974. ADOMET_ACTIVATION. 1 hit.
PS51332. B12_BINDING. 1 hit.
PS51337. B12_BINDING_NTER. 1 hit.
PS50970. HCY. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6H5Y3-1 [UniParc]FASTAAdd to Basket

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MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEEHFQG QEFKDHSRPL     50
KGNNDILSIT QPDIIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL 100
AYRMNKCSAD VARKAAEEIT LQTGVKRFVA GALGPTNKTL SVSPSVERPD 150
YRNITFDELV DAYQEQAKGL LDGRVDILLI ETIFDTANAK AALFAIQNLF 200
EENYAPPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD PLCIGLNCSL 250
GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPS TMATHLKDFA 300
VDGLVNIVGG CCGSTPDHIR EIAEAVKKCK PRVPPASVFE GHMLLSGLEP 350
FRIGPYTNFV NIGERCNVAG SRKFAKLIMA GNYEEALSIA KAQVEMGAQV 400
LDINMDDGML DGPSAMTRFC NSIASEPDIA KVPLCIDSSN FAVIEAGLKC 450
CQGKCIVNSI SLKEGEGDFL EKARKIKKFG AAVVVMAFDE EGQATETDVK 500
VNVCTRAYHL LVDKVGFNPN DIIFDPNILT IGTGMEEHNL YAINFIHATR 550
VIKETLPGVR ISGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKFGMDMGIV 600
NAGNLPVYDA IHKDLLQLCE DLIWNKDSEA TEKLLRYAQT HGTGGKKVIQ 650
TDEWRNGSIE ERLEYALVKG IEKHIVEDTE EARLNGEKYP RPLNIIEGPL 700
MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREEARLIN 750
GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV GVVLACNNFR VIDLGVMTPC 800
DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI KIPLLIGGAT 850
TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLR DDYFEEILEE 900
YEDIRQDHYE SLKERKYVPL SQARKHGFHI DWLSEPHPVK PTFIGTQVFE 950
DYNLQKLVDY IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYND 1000
AQNMLNILIS QKKLQARGVV GFWPAQSVQD DIHLYAEGVV PQAAEPIATF 1050
YGLRQQAEKD SSSTDPYHCL SDFIAPLHSG VCDYLGLFAV ACFGVEELSK 1100
TYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY SRSEQLGVPD 1150
LRRLRYEGIR PAPGYPSQPD HTEKLTMWRL ASIEQATGIR LTESLAMAPA 1200
SAVSGLYFSN VKAKYFAVGK ISKDQTEDYA LRKNMPVAEV EKWLGPILGY 1250
DTD 1253
Length:1,253
Mass (Da):139,069
Last modified:July 24, 2007 - v1
Checksum:i5507CAD9F9522537
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti343 – 3431M → L in BAE24997. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC145683 mRNA. Translation: AAI45684.1.
BC145685 mRNA. Translation: AAI45686.1.
AK142258 mRNA. Translation: BAE24997.1.
CCDSiCCDS36591.1.
RefSeqiNP_001074597.1. NM_001081128.3.
UniGeneiMm.40335.

Genome annotation databases

EnsembliENSMUST00000099856; ENSMUSP00000097442; ENSMUSG00000021311.
GeneIDi238505.
KEGGimmu:238505.
UCSCiuc007plh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC145683 mRNA. Translation: AAI45684.1 .
BC145685 mRNA. Translation: AAI45686.1 .
AK142258 mRNA. Translation: BAE24997.1 .
CCDSi CCDS36591.1.
RefSeqi NP_001074597.1. NM_001081128.3.
UniGenei Mm.40335.

3D structure databases

ProteinModelPortali A6H5Y3.
SMRi A6H5Y3. Positions 4-639, 653-908, 914-1252.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL3188.

PTM databases

PhosphoSitei A6H5Y3.

Proteomic databases

MaxQBi A6H5Y3.
PaxDbi A6H5Y3.
PRIDEi A6H5Y3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000099856 ; ENSMUSP00000097442 ; ENSMUSG00000021311 .
GeneIDi 238505.
KEGGi mmu:238505.
UCSCi uc007plh.2. mouse.

Organism-specific databases

CTDi 4548.
MGIi MGI:894292. Mtr.

Phylogenomic databases

eggNOGi COG1410.
GeneTreei ENSGT00420000029824.
HOGENOMi HOG000251409.
HOVERGENi HBG006347.
InParanoidi A6H5Y3.
KOi K00548.
OMAi LTEHYAM.
OrthoDBi EOG7TF786.
PhylomeDBi A6H5Y3.
TreeFami TF312829.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .
Reactomei REACT_189091. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
REACT_189092. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_202492. Sulfur amino acid metabolism.

Miscellaneous databases

NextBioi 383806.
PROi A6H5Y3.
SOURCEi Search...

Gene expression databases

Bgeei A6H5Y3.
Genevestigatori A6H5Y3.

Family and domain databases

Gene3Di 1.10.1240.10. 1 hit.
3.10.196.10. 1 hit.
3.20.20.20. 1 hit.
3.20.20.330. 1 hit.
3.40.50.280. 1 hit.
InterProi IPR003759. Cbl-bd_cap.
IPR006158. Cobalamin-bd.
IPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
IPR003726. S_MeTrfase.
IPR004223. VitB12-dep_Met_synth_activ_dom.
[Graphical view ]
Pfami PF02310. B12-binding. 1 hit.
PF02607. B12-binding_2. 1 hit.
PF02965. Met_synt_B12. 1 hit.
PF00809. Pterin_bind. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view ]
PIRSFi PIRSF000381. MetH. 1 hit.
SMARTi SM01018. B12-binding_2. 1 hit.
[Graphical view ]
SUPFAMi SSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsi TIGR02082. metH. 1 hit.
PROSITEi PS50974. ADOMET_ACTIVATION. 1 hit.
PS51332. B12_BINDING. 1 hit.
PS51337. B12_BINDING_NTER. 1 hit.
PS50970. HCY. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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].
    Tissue: Brain.
  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] OF 1-738.
    Strain: C57BL/6J.
    Tissue: Heart.

Entry informationi

Entry nameiMETH_MOUSE
AccessioniPrimary (citable) accession number: A6H5Y3
Secondary accession number(s): Q3UQP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: September 3, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

L-homocysteine is bound via the zinc atom By similarity.

Keywords - Technical termi

Complete proteome, 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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