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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).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi260 – 2601ZincPROSITE-ProRule annotation
Metal bindingi323 – 3231ZincPROSITE-ProRule annotation
Metal bindingi324 – 3241ZincPROSITE-ProRule annotation
Metal bindingi785 – 7851Cobalt (cobalamin axial ligand)By similarity
Binding sitei830 – 8301CobalaminBy similarity
Binding sitei974 – 9741S-adenosyl-L-methionineBy similarity
Binding sitei1172 – 11721S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei1176 – 11761Cobalamin; via carbonyl oxygenBy 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-KW
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 338320Hcy-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini371 – 632262Pterin-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini662 – 75998B12-binding N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini772 – 907136B12-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini923 – 1265343AdoMet activationPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni860 – 8612Cobalamin-bindingBy similarity
Regioni1227 – 12282S-adenosyl-L-methionine bindingBy 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).By similarity

Sequence similaritiesi

Contains 1 AdoMet activation domain.PROSITE-ProRule annotation
Contains 1 B12-binding domain.PROSITE-ProRule annotation
Contains 1 Hcy-binding domain.PROSITE-ProRule annotation
Contains 1 pterin-binding domain.PROSITE-ProRule annotation

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

« Hide

        10         20         30         40         50
MAPTLQDLTP SAGMKKTLQD EIEAILQERI MVLDGGMGTM IQRHKLSEED
60 70 80 90 100
FRGQEFKDHA RPLKGNNDIL SITQPNVIYQ IHKEYLLAGA DIIETNTFSS
110 120 130 140 150
TSIAQADYGL EHLAYRMNMC SAGVARKAAE DISLQTGIKR YVAGALGPTN
160 170 180 190 200
KTLSVSPSVE RPDYRNITFD ELVEAYKEQA KGLLDGGVDI LLIETIFDTA
210 220 230 240 250
NAKAALFAVQ KLFEEEYVPR PVFISGTIVD KSGRTLSGQT GEAFVISVSH
260 270 280 290 300
ADPLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET
310 320 330 340 350
PHVMAMHLKD FAVDGLVNIV GGCCGTTPDH IREIAEAVKN CKPRVPPATV
360 370 380 390 400
FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRRFAKLI MAGNYEEALS
410 420 430 440 450
VAKMQVEMGA QVLDINMDDG MLDGPSAMTR FCNFIASEPD IAKVPLCIDS
460 470 480 490 500
SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK FGAAVVVMAF
510 520 530 540 550
DEEGQATETD PKIRVCTRAY HLLLKKLGFN PNDIIFDPNI LTIGTGMEEH
560 570 580 590 600
NLYAVNFINA TKVIKETLPG AKVSGGLSNL SFSFRGMEAI REAMHGVFLY
610 620 630 640 650
HAIKFGMDMG IVNAGSLPVY DDIHKELLQL CEDLIWNRDP EATEKLLHYA
660 670 680 690 700
QTQGKGGKKV IQTDEWRNGP LEERLEYALV KGIEKYIIED TEEARLNQEK
710 720 730 740 750
YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF
760 770 780 790 800
MEKEREETKV LTGKIEDEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN
810 820 830 840 850
FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL
860 870 880 890 900
AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN
910 920 930 940 950
LKDEYFEEIL EEYEDIRQDH YESLKERRYL TLRQARENGF HIDWLSEPPP
960 970 980 990 1000
VKPTFLGTRV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFDDK
1010 1020 1030 1040 1050
TVGEEAKKVY DDAQNMLQAL ISQKKLQARG VVGFWPAQSI QDDIHLYAEG
1060 1070 1080 1090 1100
AVPQASEPIA TFYGLRQQAE KDSASSDPYL CLSDFIAPLH SGIPDYLGLF
1110 1120 1130 1140 1150
AVACFGVEEL SKAYEEECDD YSSIMVKALG DRLAEAFAEE LHERARRELW
1160 1170 1180 1190 1200
GYCSGEQLAV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTVW RLADVEQRTG
1210 1220 1230 1240 1250
IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQIED YASRKNMSVA
1260
EVEKWLGPIL GYDTD
Length:1,265
Mass (Da):140,478
Last modified:August 2, 2005 - v1
Checksum:i7E1E03AB95134529
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3