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Q9Z2Q4

- METH_RAT

UniProt

Q9Z2Q4 - METH_RAT

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Protein
Methionine synthase
Gene
Mtr
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 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. amino acid binding Source: RGD
  3. cobalamin binding Source: RGD
  4. folic acid binding Source: RGD
  5. methionine synthase activity Source: RGD
  6. methyltransferase activity Source: RGD
  7. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. homocysteine metabolic process Source: RGD
  2. methionine biosynthetic process Source: RGD
  3. methionine metabolic process Source: RGD
  4. protein methylation Source: RGD
  5. tetrahydrofolate metabolic process Source: RGD
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

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621283. 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_0000312902Add
BLAST

Proteomic databases

PaxDbiQ9Z2Q4.
PRIDEiQ9Z2Q4.

PTM databases

PhosphoSiteiQ9Z2Q4.

Expressioni

Gene expression databases

GenevestigatoriQ9Z2Q4.

Interactioni

Protein-protein interaction databases

BioGridi249519. 1 interaction.
IntActiQ9Z2Q4. 1 interaction.
STRINGi10116.ENSRNOP00000023973.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2Q4.
SMRiQ9Z2Q4. Positions 652-908, 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.
HOGENOMiHOG000251409.
HOVERGENiHBG006347.
InParanoidiQ9Z2Q4.
KOiK00548.
PhylomeDBiQ9Z2Q4.

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.

Q9Z2Q4-1 [UniParc]FASTAAdd to Basket

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MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEENFQG QEFKDHSRPL     50
KGNNDILSIT QPDVIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL 100
AYRMNKCSAD VARKAAEEIT LQTGVKRFVA GSLGPTNKTL SVSPSVERPD 150
YRNITFDELV EAYQEQAKGL LDGGVDILLI ETIFDTANAK AALFALQKLF 200
EENYASPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD PLCIGLNCAL 250
GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPA MMAMHLKDFA 300
VDGLVNVVGG CCGSTPDHIR EIAEAVKNCK PRVPPDSVFE GHMLLSGLEP 350
FRIGPYTNFV NIGERCNVAG SKKFAKLIMA GNYEEALSVA KVQVEMGAQV 400
LDINMDDGML DGPSAMTKFC NFIASEPDIA KVPLCIDSSN FAVIEAGLKC 450
CQGKCIVNSI SLKEGEEDFL EKARKIKKFG AAVVVMAFDE EGQATETDVK 500
VSVCTRAYHL LVEKVGFNPN DIIFDPNILT IGTGMEEHNL YAINFIHATR 550
VIKETLPGVR ISGGLSNLSF AFRGMDAIRE AMHGVFLYHA IKFGMDMGIV 600
NAGSLPVYDD IHKDLLQLCE DLIWNRDAEA TEKLLRYAQT HGKGGKKVIQ 650
TDEWRNGSIE ERLEYALVKG IEKHIVEDTE EARLNREKYP RPLNIIEGPL 700
MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREEARVLN 750
GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMTPC 800
DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI KIPLLIGGAT 850
TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLK DDYFEEILEE 900
YEDIRQDHYE SLKERKYLPL SQARKHSFHI DWLSEPHPVK PTFIGTQVFE 950
DYNLQKLVDY IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYED 1000
AQNMLSILIS RKKLRARGVV GFWPAQSVQD DIHLYAEGAV PQAAEPIATF 1050
YGLRQQAEKD SSSTDPYHCL SDFVAPLHSG VRDYLGLFAV ACFGVEELSK 1100
AYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY CGSEQLGVTD 1150
LRKLRYEGIR PAPGYPSQPD HTEKLTMWRL ANIEQATGIR LTESLAMAPA 1200
SAVSGLYFSN VKSKYFAVGK ISKDQIEDYA LRKNMSVAEV EKWLGPILGY 1250
DTD 1253
Length:1,253
Mass (Da):139,164
Last modified:May 1, 1999 - v1
Checksum:i96BD40B796EBD75B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF034214 mRNA. Translation: AAD05384.1.
PIRiT42376.
RefSeqiNP_110491.1. NM_030864.1.
UniGeneiRn.205061.

Genome annotation databases

GeneIDi81522.
KEGGirno:81522.
UCSCiRGD:621283. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF034214 mRNA. Translation: AAD05384.1 .
PIRi T42376.
RefSeqi NP_110491.1. NM_030864.1.
UniGenei Rn.205061.

3D structure databases

ProteinModelPortali Q9Z2Q4.
SMRi Q9Z2Q4. Positions 652-908, 914-1252.
ModBasei Search...

Protein-protein interaction databases

BioGridi 249519. 1 interaction.
IntActi Q9Z2Q4. 1 interaction.
STRINGi 10116.ENSRNOP00000023973.

PTM databases

PhosphoSitei Q9Z2Q4.

Proteomic databases

PaxDbi Q9Z2Q4.
PRIDEi Q9Z2Q4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 81522.
KEGGi rno:81522.
UCSCi RGD:621283. rat.

Organism-specific databases

CTDi 4548.
RGDi 621283. Mtr.

Phylogenomic databases

eggNOGi COG1410.
HOGENOMi HOG000251409.
HOVERGENi HBG006347.
InParanoidi Q9Z2Q4.
KOi K00548.
PhylomeDBi Q9Z2Q4.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .

Miscellaneous databases

NextBioi 615041.
PROi Q9Z2Q4.

Gene expression databases

Genevestigatori Q9Z2Q4.

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. "Cloning, sequencing, and heterologous expression of rat methionine synthase cDNA."
    Yamada K., Tobimatsu T., Toraya T.
    Biosci. Biotechnol. Biochem. 62:2155-2160(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.

Entry informationi

Entry nameiMETH_RAT
AccessioniPrimary (citable) accession number: Q9Z2Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 96 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi