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Q4JIJ3

- METH_BOVIN

UniProt

Q4JIJ3 - METH_BOVIN

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Protein

Methionine synthase

Gene
MTR
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 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 bindingi260 – 2601Zinc By similarity
Metal bindingi323 – 3231Zinc By similarity
Metal bindingi324 – 3241Zinc By similarity
Metal bindingi785 – 7851Cobalt (cobalamin axial ligand) By similarity
Binding sitei830 – 8301Cobalamin By similarity
Binding sitei974 – 9741S-adenosyl-L-methionine By similarity
Binding sitei1172 – 11721S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei1176 – 11761Cobalamin; via carbonyl oxygen By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. 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

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

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 – 12651265Methionine synthasePRO_0000251734Add
BLAST

Proteomic databases

PRIDEiQ4JIJ3.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016262.

Structurei

3D structure databases

ProteinModelPortaliQ4JIJ3.
SMRiQ4JIJ3. Positions 664-920, 926-1264.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 338320Hcy-bindingAdd
BLAST
Domaini371 – 632262Pterin-bindingAdd
BLAST
Domaini662 – 75998B12-binding N-terminalAdd
BLAST
Domaini772 – 907136B12-bindingAdd
BLAST
Domaini923 – 1265343AdoMet activationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni860 – 8612Cobalamin-binding By similarity
Regioni1227 – 12282S-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.
InParanoidiQ4JIJ3.
KOiK00548.

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.

Q4JIJ3-1 [UniParc]FASTAAdd to Basket

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MAPTLQDLTP SAGMKKTLQD EIEAILQERI MVLDGGMGTM IQRHKLSEED     50
FRGQEFKDHA RPLKGNNDIL SITQPNVIYQ IHKEYLLAGA DIIETNTFSS 100
TSIAQADYGL EHLAYRMNMC SAGVARKAAE DISLQTGIKR YVAGALGPTN 150
KTLSVSPSVE RPDYRNITFD ELVEAYKEQA KGLLDGGVDI LLIETIFDTA 200
NAKAALFAVQ KLFEEEYVPR PVFISGTIVD KSGRTLSGQT GEAFVISVSH 250
ADPLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET 300
PHVMAMHLKD FAVDGLVNIV GGCCGTTPDH IREIAEAVKN CKPRVPPATV 350
FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRRFAKLI MAGNYEEALS 400
VAKMQVEMGA QVLDINMDDG MLDGPSAMTR FCNFIASEPD IAKVPLCIDS 450
SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK FGAAVVVMAF 500
DEEGQATETD PKIRVCTRAY HLLLKKLGFN PNDIIFDPNI LTIGTGMEEH 550
NLYAVNFINA TKVIKETLPG AKVSGGLSNL SFSFRGMEAI REAMHGVFLY 600
HAIKFGMDMG IVNAGSLPVY DDIHKELLQL CEDLIWNRDP EATEKLLHYA 650
QTQGKGGKKV IQTDEWRNGP LEERLEYALV KGIEKYIIED TEEARLNQEK 700
YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF 750
MEKEREETKV LTGKIEDEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN 800
FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL 850
AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN 900
LKDEYFEEIL EEYEDIRQDH YESLKERRYL TLRQARENGF HIDWLSEPPP 950
VKPTFLGTRV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFDDK 1000
TVGEEAKKVY DDAQNMLQAL ISQKKLQARG VVGFWPAQSI QDDIHLYAEG 1050
AVPQASEPIA TFYGLRQQAE KDSASSDPYL CLSDFIAPLH SGIPDYLGLF 1100
AVACFGVEEL SKAYEEECDD YSSIMVKALG DRLAEAFAEE LHERARRELW 1150
GYCSGEQLAV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTVW RLADVEQRTG 1200
IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQIED YASRKNMSVA 1250
EVEKWLGPIL GYDTD 1265
Length:1,265
Mass (Da):140,478
Last modified:August 2, 2005 - v1
Checksum:i7E1E03AB95134529
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ084519 mRNA. Translation: AAY86762.1.
RefSeqiNP_001025469.1. NM_001030298.1.
UniGeneiBt.47673.

Genome annotation databases

GeneIDi280869.
KEGGibta:280869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ084519 mRNA. Translation: AAY86762.1 .
RefSeqi NP_001025469.1. NM_001030298.1.
UniGenei Bt.47673.

3D structure databases

ProteinModelPortali Q4JIJ3.
SMRi Q4JIJ3. Positions 664-920, 926-1264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000016262.

Proteomic databases

PRIDEi Q4JIJ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 280869.
KEGGi bta:280869.

Organism-specific databases

CTDi 4548.

Phylogenomic databases

eggNOGi COG1410.
HOGENOMi HOG000251409.
HOVERGENi HBG006347.
InParanoidi Q4JIJ3.
KOi K00548.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .

Miscellaneous databases

NextBioi 20805009.

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. "Interactions of folic acid-vitamin B12-methionine: effects on liver metabolism and production of dairy cows."
    Palin M.-F., Beaudry D., Charest R., Girard C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiMETH_BOVIN
AccessioniPrimary (citable) accession number: Q4JIJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: August 2, 2005
Last modified: July 9, 2014
This is version 69 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