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Q4JIJ3 (METH_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine synthase

EC=2.1.1.13
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Vitamin-B12 dependent methionine synthase
Short name=MS
Gene names
Name:MTR
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length1265 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Cofactor

Methylcobalamin (MeCBL) By similarity.

Binds 1 zinc ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.

Subcellular location

Cytoplasm By similarity.

Domain

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.

Miscellaneous

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

Sequence similarities

Belongs to the vitamin-B12 dependent methionine synthase family.

Contains 1 AdoMet activation domain.

Contains 1 B12-binding domain.

Contains 1 B12-binding N-terminal domain.

Contains 1 Hcy-binding domain.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12651265Methionine synthase
PRO_0000251734

Regions

Domain19 – 338320Hcy-binding
Domain371 – 632262Pterin-binding
Domain662 – 75998B12-binding N-terminal
Domain772 – 907136B12-binding
Domain923 – 1265343AdoMet activation
Region860 – 8612Cobalamin-binding By similarity
Region1227 – 12282S-adenosyl-L-methionine binding By similarity

Sites

Metal binding2601Zinc By similarity
Metal binding3231Zinc By similarity
Metal binding3241Zinc By similarity
Metal binding7851Cobalt (cobalamin axial ligand) By similarity
Binding site8301Cobalamin By similarity
Binding site9741S-adenosyl-L-methionine By similarity
Binding site11721S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site11761Cobalamin; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4JIJ3 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 7E1E03AB95134529

FASTA1,265140,478
        10         20         30         40         50         60 
MAPTLQDLTP SAGMKKTLQD EIEAILQERI MVLDGGMGTM IQRHKLSEED FRGQEFKDHA 

        70         80         90        100        110        120 
RPLKGNNDIL SITQPNVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC 

       130        140        150        160        170        180 
SAGVARKAAE DISLQTGIKR YVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYKEQA 

       190        200        210        220        230        240 
KGLLDGGVDI LLIETIFDTA NAKAALFAVQ KLFEEEYVPR PVFISGTIVD KSGRTLSGQT 

       250        260        270        280        290        300 
GEAFVISVSH ADPLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET 

       310        320        330        340        350        360 
PHVMAMHLKD FAVDGLVNIV GGCCGTTPDH IREIAEAVKN CKPRVPPATV FEGHMLLSGL 

       370        380        390        400        410        420 
EPFRIGPYTN FVNIGERCNV AGSRRFAKLI MAGNYEEALS VAKMQVEMGA QVLDINMDDG 

       430        440        450        460        470        480 
MLDGPSAMTR FCNFIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD 

       490        500        510        520        530        540 
FLEKARKIKK FGAAVVVMAF DEEGQATETD PKIRVCTRAY HLLLKKLGFN PNDIIFDPNI 

       550        560        570        580        590        600 
LTIGTGMEEH NLYAVNFINA TKVIKETLPG AKVSGGLSNL SFSFRGMEAI REAMHGVFLY 

       610        620        630        640        650        660 
HAIKFGMDMG IVNAGSLPVY DDIHKELLQL CEDLIWNRDP EATEKLLHYA QTQGKGGKKV 

       670        680        690        700        710        720 
IQTDEWRNGP LEERLEYALV KGIEKYIIED TEEARLNQEK YPRPLNIIEG PLMNGMKIVG 

       730        740        750        760        770        780 
DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETKV LTGKIEDEDP YQGTIVLATV 

       790        800        810        820        830        840 
KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM 

       850        860        870        880        890        900 
IFVAKEMERL AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN 

       910        920        930        940        950        960 
LKDEYFEEIL EEYEDIRQDH YESLKERRYL TLRQARENGF HIDWLSEPPP VKPTFLGTRV 

       970        980        990       1000       1010       1020 
FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFDDK TVGEEAKKVY DDAQNMLQAL 

      1030       1040       1050       1060       1070       1080 
ISQKKLQARG VVGFWPAQSI QDDIHLYAEG AVPQASEPIA TFYGLRQQAE KDSASSDPYL 

      1090       1100       1110       1120       1130       1140 
CLSDFIAPLH SGIPDYLGLF AVACFGVEEL SKAYEEECDD YSSIMVKALG DRLAEAFAEE 

      1150       1160       1170       1180       1190       1200 
LHERARRELW GYCSGEQLAV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTVW RLADVEQRTG 

      1210       1220       1230       1240       1250       1260 
IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQIED YASRKNMSVA EVEKWLGPIL 


GYDTD 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ084519 mRNA. Translation: AAY86762.1.
RefSeqNP_001025469.1. NM_001030298.1.
UniGeneBt.47673.

3D structure databases

ProteinModelPortalQ4JIJ3.
SMRQ4JIJ3. Positions 664-920, 926-1264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000016262.

Proteomic databases

PRIDEQ4JIJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID280869.
KEGGbta:280869.

Organism-specific databases

CTD4548.

Phylogenomic databases

eggNOGCOG1410.
HOGENOMHOG000251409.
HOVERGENHBG006347.
InParanoidQ4JIJ3.
KOK00548.

Enzyme and pathway databases

UniPathwayUPA00051; UER00081.

Family and domain databases

Gene3D1.10.1240.10. 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.
InterProIPR003759. 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]
PfamPF02310. 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]
PIRSFPIRSF000381. MetH. 1 hit.
SMARTSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsTIGR02082. metH. 1 hit.
PROSITEPS50974. 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]
ProtoNetSearch...

Other

NextBio20805009.

Entry information

Entry nameMETH_BOVIN
AccessionPrimary (citable) accession number: Q4JIJ3
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways