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O50008 (METE_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
EC=2.1.1.14
Alternative name(s):
Cobalamin-independent methionine synthase isozyme
Vitamin-B12-independent methionine synthase isozyme
Gene names
Name:CIMS
Ordered Locus Names:At5g17920
ORF Names:MPI7.9
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length765 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.

Catalytic activity

5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine.

Cofactor

Zinc By similarity.

Pathway

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

Subcellular location

Cytoplasm Potential.

Post-translational modification

Ubiquitinated. Ref.6

Sequence similarities

Belongs to the vitamin-B12 independent methionine synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7657655-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
PRO_0000098696

Sites

Metal binding6471Zinc By similarity
Metal binding6491Zinc By similarity
Metal binding7331Zinc By similarity

Amino acid modifications

Cross-link406Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6

Secondary structure

1 .......................................................................................................................... 765
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O50008 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 2EA01908B5951154

FASTA76584,357
        10         20         30         40         50         60 
MASHIVGYPR MGPKRELKFA LESFWDGKST AEDLQKVSAD LRSSIWKQMS AAGTKFIPSN 

        70         80         90        100        110        120 
TFAHYDQVLD TTAMLGAVPP RYGYTGGEIG LDVYFSMARG NASVPAMEMT KWFDTNYHYI 

       130        140        150        160        170        180 
VPELGPEVNF SYASHKAVNE YKEAKALGVD TVPVLVGPVS YLLLSKAAKG VDKSFELLSL 

       190        200        210        220        230        240 
LPKILPIYKE VITELKAAGA TWIQLDEPVL VMDLEGQKLQ AFTGAYAELE STLSGLNVLV 

       250        260        270        280        290        300 
ETYFADIPAE AYKTLTSLKG VTAFGFDLVR GTKTLDLVKA GFPEGKYLFA GVVDGRNIWA 

       310        320        330        340        350        360 
NDFAASLSTL QALEGIVGKD KLVVSTSCSL LHTAVDLINE TKLDDEIKSW LAFAAQKVVE 

       370        380        390        400        410        420 
VNALAKALAG QKDEALFSAN AAALASRRSS PRVTNEGVQK AAAALKGSDH RRATNVSARL 

       430        440        450        460        470        480 
DAQQKKLNLP ILPTTTIGSF PQTVELRRVR REYKAKKVSE EDYVKAIKEE IKKVVDLQEE 

       490        500        510        520        530        540 
LDIDVLVHGE PERNDMVEYF GEQLSGFAFT ANGWVQSYGS RCVKPPVIYG DVSRPKAMTV 

       550        560        570        580        590        600 
FWSAMAQSMT SRPMKGMLTG PVTILNWSFV RNDQPRHETC YQIALAIKDE VEDLEKGGIG 

       610        620        630        640        650        660 
VIQIDEAALR EGLPLRKSEH AFYLDWAVHS FRITNCGVQD STQIHTHMCY SHFNDIIHSI 

       670        680        690        700        710        720 
IDMDADVITI ENSRSDEKLL SVFREGVKYG AGIGPGVYDI HSPRIPSSEE IADRVNKMLA 

       730        740        750        760 
VLEQNILWVN PDCGLKTRKY TEVKPALKNM VDAAKLIRSQ LASAK

« Hide

References

« Hide 'large scale' references
[1]"The specific features of methionine biosynthesis and metabolism in plants."
Ravanel S., Gakiere B., Job D., Douce R.
Proc. Natl. Acad. Sci. U.S.A. 95:7805-7812(1998) [PubMed: 9636232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Strain: cv. Columbia.
[2]"Characterization of the cDNA and gene for a cytosolic cobalamin-independent methionine synthase in Arabidopsis thaliana."
Gakiere B., Job D., Douce R., Ravanel S.
Plant Gene Register PGR99-115
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones."
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S.
DNA Res. 5:131-145(1998) [PubMed: 9679202] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
Plant J. 59:344-358(2009) [PubMed: 19292762] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-406, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U97200 mRNA. Translation: AAC50037.1.
AB011480 Genomic DNA. Translation: BAB11226.1.
CP002688 Genomic DNA. Translation: AED92486.1.
CP002688 Genomic DNA. Translation: AED92487.1.
AF370522 mRNA. Translation: AAK43899.1.
AY048201 mRNA. Translation: AAK82464.1.
AY056098 mRNA. Translation: AAL06986.1.
AY057499 mRNA. Translation: AAL09740.1.
AY069876 mRNA. Translation: AAL47432.1.
AY070771 mRNA. Translation: AAL50108.1.
AY091692 mRNA. Translation: AAM10291.1.
IPIIPI00522440.
RefSeqNP_001078599.1. NM_001085130.1.
NP_197294.1. NM_121798.3.
UniGeneAt.22340.
At.71028.
At.74794.
At.74941.
At.74999.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U1HX-ray2.55A1-765[»]
1U1JX-ray2.40A1-765[»]
1U1UX-ray2.95A1-765[»]
1U22X-ray2.65A1-765[»]
ProteinModelPortalO50008.
SMRO50008. Positions 2-760.
ModBaseSearch...

Protein-protein interaction databases

IntActO50008. 1 interaction.
STRINGO50008.

2D gel databases

SWISS-2DPAGEO50008.

Proteomic databases

PRIDEO50008.
ProMEXO50008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G17920.1; AT5G17920.1; AT5G17920.
AT5G17920.2; AT5G17920.2; AT5G17920.
GeneID831660.
GenomeReviewsGene locus AT5G17920 in contig BA000015_GR.
KEGGath:AT5G17920.
NMPDRfig|3702.1.peg.23963.

Organism-specific databases

TAIRAt5g17920.

Phylogenomic databases

eggNOGKOG2263.
HOGENOMHBG287495.
InParanoidO50008.
OMANIWANDF.
PhylomeDBO50008.
ProtClustDBPLN02475.

Enzyme and pathway databases

BRENDA2.1.1.14. 399.

Gene expression databases

GenevestigatorO50008.
GermOnlineAT5G17920. Arabidopsis thaliana.

Family and domain databases

InterProIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Methionine_synth.
[Graphical view]
KOK00549.
PfamPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFPIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMsTIGR01371. Met_syn_B12ind. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMETE_ARATH
AccessionPrimary (citable) accession number: O50008
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: November 16, 2011
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents