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A8XY95 (METH_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 48. 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:
Probable 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:metr-1
ORF Names:CBG20636
OrganismCaenorhabditis briggsae [Reference proteome]
Taxonomic identifier6238 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length1273 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

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 – 12731273Probable methionine synthase
PRO_0000412913

Regions

Domain7 – 327321Hcy-binding
Domain360 – 621262Pterin-binding
Domain652 – 74998B12-binding N-terminal
Domain762 – 897136B12-binding
Domain927 – 1273347AdoMet activation
Region850 – 8512Cobalamin-binding By similarity
Region1225 – 12262S-adenosyl-L-methionine binding By similarity

Sites

Metal binding2491Zinc By similarity
Metal binding3121Zinc By similarity
Metal binding3131Zinc By similarity
Metal binding7751Cobalt (cobalamin axial ligand) By similarity
Binding site8201Cobalamin By similarity
Binding site9771S-adenosyl-L-methionine By similarity
Binding site11711S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site11751Cobalamin; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A8XY95 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 7178233645CE06AE

FASTA1,273141,762
        10         20         30         40         50         60 
MTRSSLFKEL ADIAKERIMI IDGAMGTMIQ REYMEEHDFR GEILKDHDKP LKGNNDLLSI 

        70         80         90        100        110        120 
TRPDIIYKIH KLYLEAGADF IETNTFSGTT IAQADYHCEH LVHEINYQSA LVARRACDDV 

       130        140        150        160        170        180 
GAATGIRRYV CGAIGPTNRT LSISPSVEKP DFRNVTFQEL VKAYGDQARS LIQGGVDVLL 

       190        200        210        220        230        240 
VETVFDSANA KAALFAIRTL FEDEGVPEIP VFLSGTIVDM SGRTLSGQTG EAFLVSTKQG 

       250        260        270        280        290        300 
KPIAVGLNCA LGAKDMRQFV QNMSLWSDTL ILCYPNAGLP NALGGYDETP EEMAEVLREF 

       310        320        330        340        350        360 
AQDGLVNIIG GCCGTTPDHI NAMYKAVQGI SPRVPPADPH AGKMLLSGLE PSIVGPETNF 

       370        380        390        400        410        420 
VNIGERCNVA GSRRFCNLIK NENYDTAIDV ARVQVDSGAQ ILDVNMDDGL LDGPYAMSKF 

       430        440        450        460        470        480 
LRLISSEPDV AKIPVCIDSS DFDVIIAGLE STQGKCVVNS ISLKEGEEKF KERARIVKRY 

       490        500        510        520        530        540 
GAAVVVMAFD EEGQAAETER KFEICERSYR ILTEEVGFNP NDIIFDANIL TIATGMDEHA 

       550        560        570        580        590        600 
NYGMYFIEAT RMIRENLPGA HVSGGVSNIS FSFRGMEAIR EAMHSVFLFY AIKAGMDMGI 

       610        620        630        640        650        660 
VNAGALPVYE DIDKPLLQLL EDLLFNRDPE ATEKLLVAAQ EMKKDGKKAD TKTDEWRNTS 

       670        680        690        700        710        720 
VEERLKFALV KGIDQFVVAD TEEARQNTEK YPRPLNVIER PLMDGMAVVG ELFGAGKMFL 

       730        740        750        760        770        780 
PQVIKSARVM KKAVAHLLPF MDAERQANIE KMGLDEDESP YQGTVVIATV KGDVHDIGKN 

       790        800        810        820        830        840 
IVAVVLGCNN FKVVDLGVMT PCENIIKAAI EEKADFIGLS GLITPSLDEM VHVAKEMNRV 

       850        860        870        880        890        900 
GLKIPLLIGG ATTSKTHTAV KIAPRYPHPV VHCLDASKSV VVCSSLSDMT VRDAFLQDLN 

       910        920        930        940        950        960 
EDYEDVRTKM CLVSYLNHFF ITEHYESLKD RRFVALGKTR EKKFNIDWNK FSPVKPSFIG 

       970        980        990       1000       1010       1020 
RREFQNFDFK ELIPYIDWKP FFDVWQLRGK YPNRSYPKIF DDADVGGEAK RVFDDAQTWL 

      1030       1040       1050       1060       1070       1080 
KKLIDEKVLT ANAVVSFLPA ASEGDDIHVY DPETGNKLDT FYGLRQQSGR EHDQSHFCLS 

      1090       1100       1110       1120       1130       1140 
DFIRPLKIGV PDDYLGLFAC TAGLGAEEYC KVLEENHDDY ASIMVKALAD RLAEAYAEYL 

      1150       1160       1170       1180       1190       1200 
HKEVRVNLWG YSTNEQLTET DLLSIKYEGI RPACGYPSQP DHTEKRTLWK LLEAEKNGIV 

      1210       1220       1230       1240       1250       1260 
LTEHLAMLPA ASVSGLYFAN PQSQYFAVGK IDEDQVAFIY VRSKNVTDYA ARKNVPKEEV 

      1270 
ERWLSPIIGY ELD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE600991 Genomic DNA. Translation: CAP37612.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6238.CBG20636.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaCBG20636; CBG20636; CBG20636.

Organism-specific databases

WormBaseCBG20636; CBP26766; WBGene00039583; Cbr-metr-1.

Phylogenomic databases

eggNOGCOG1410.
HOGENOMHOG000251409.
OrthoDBEOG7TF786.

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...

Entry information

Entry nameMETH_CAEBR
AccessionPrimary (citable) accession number: A8XY95
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways