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Q09582 (METH_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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:nos-1
ORF Names:R03D7.1
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length1249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Y76A2B.5Q9XWC91EBI-331777,EBI-331773

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12491249Probable methionine synthase
PRO_0000204531

Regions

Domain1 – 327327Hcy-binding
Domain360 – 621262Pterin-binding
Domain652 – 74998B12-binding N-terminal
Domain762 – 897136B12-binding
Domain913 – 1249337AdoMet activation
Region850 – 8512Cobalamin-binding By similarity
Region1211 – 12122S-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 site9631S-adenosyl-L-methionine By similarity
Binding site11571S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site11611Cobalamin; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q09582 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4D16028AD02CD550

FASTA1,249138,899
        10         20         30         40         50         60 
MTRSSLFEEL AEIAKERIMI IDGAMGTMIQ REYMEEEDFR GEILKDHDKP LKGNNDLLSI 

        70         80         90        100        110        120 
TRPDIIYKIH KLYLEAGADF VETNTFSGTT IAQADYRCEH LVHEINYQSA LVARRACDDV 

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

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

       250        260        270        280        290        300 
KPMAVGLNCA LGAKDMRQFV DNMSKWSDSF IICYPNAGLP NALGGYDETP EEMADVLREF 

       310        320        330        340        350        360 
ARDGLVNIIG GCCGTTPDHI NAMYKAVQGI TPRVPPQDPH 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 KERARIIKRY 

       490        500        510        520        530        540 
GAAVVVMAFD EQGQAAETDP KFEICERSYR ILTEEVGFNP NDIIFDANIL TIATGMEEHS 

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

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

       670        680        690        700        710        720 
VEERLKFALV KGVDQFVVAD TEEARQNTAK YPRPLNVIER PLMDGMAVVG ELFGAGKMFL 

       730        740        750        760        770        780 
PQVIKSARVM KKAVAHLLPF MEIERQANIE TMGLAEDESP YQGTVVIATV KGDVHDIGKN 

       790        800        810        820        830        840 
IVSVVLGCNN FKVVDLGVMT PCENIIKAAI EEKADFIGLS GLITPSLDEM VYVAKEMNRV 

       850        860        870        880        890        900 
GLNIPLLIGG ATTSKTHTAV KISPRYPHPV VHCLDASKSV VVCSSLSDMS VRDAFLQDLN 

       910        920        930        940        950        960 
EDYEDVRQEH YASLKDRRFT DLNKTREKKF KIDWDKFTAV KPSFVGRREY QNFDLNELIP 

       970        980        990       1000       1010       1020 
YIDWKPFFDV WQLRGKYPNR SYPKIFDDAD VGAEAKKVFD DAQTWLKKLI DEKILVANAV 

      1030       1040       1050       1060       1070       1080 
VSFLPAASEG DDMHVYDPET GNKLDTFYGL RQQSGREHDQ PHFCLSDFIK PLKNGVPDDY 

      1090       1100       1110       1120       1130       1140 
LGLFACTAGL GAEEYCKTLE KNHDDYASIM VKALADRLAE AYAEYLHKEV RTTLWGYSTN 

      1150       1160       1170       1180       1190       1200 
EDLTESDLLS IKYQGIRPAC GYPSQPDHTE KRTLWKLLEA EKNGIGLTEH LAMLPAASVS 

      1210       1220       1230       1240 
GLYFANPQSE YFAVGKIDQD QVIDYAARKN VPKEEVERWL SPILGYDTD

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References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z46828 Genomic DNA. Translation: CAA86855.1.
PIRT23868.
RefSeqNP_496353.1. NM_063952.4.
UniGeneCel.16853.

3D structure databases

ProteinModelPortalQ09582.
SMRQ09582. Positions 9-643, 655-1249.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-26122N.
IntActQ09582. 1 interaction.
MINTMINT-1116270.
STRING6239.R03D7.1.

Proteomic databases

PaxDbQ09582.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaR03D7.1; R03D7.1; R03D7.1.
GeneID174681.
KEGGcel:CELE_R03D7.1.
UCSCR03D7.1. c. elegans.

Organism-specific databases

CTD174681.
WormBaseR03D7.1; CE01609; WBGene00010988.

Phylogenomic databases

eggNOGCOG1410.
GeneTreeENSGT00420000029824.
HOGENOMHOG000251409.
InParanoidQ09582.
KOK00548.
OMAVRKEFWG.

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]
PANTHERPTHR21091:SF9. PTHR21091:SF9. 1 hit.
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]
SUPFAMSSF52242. Cbl-bd. 1 hit.
SSF51717. DHP_synth_like. 1 hit.
SSF56507. Met_synth_B12. 1 hit.
SSF47644. Met_synth_Cbl-bd. 1 hit.
SSF82282. S_methyl_trans. 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

NextBio885042.

Entry information

Entry nameMETH_CAEEL
AccessionPrimary (citable) accession number: Q09582
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 29, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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