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A4J5C3 (METE_DESRM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

EC=2.1.1.14
Alternative name(s):
Cobalamin-independent methionine synthase
Methionine synthase, vitamin-B12 independent isozyme
Gene names
Name:metE
Ordered Locus Names:Dred_1751
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum

Protein attributes

Sequence length764 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation By similarity. HAMAP MF_00172

Catalytic activity

5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. HAMAP MF_00172

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00172

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1. HAMAP MF_00172

Sequence similarities

Belongs to the vitamin-B12 independent methionine synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7647645-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172
PRO_1000071611

Sites

Metal binding6451Zinc By similarity
Metal binding6471Zinc By similarity
Metal binding7301Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A4J5C3 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 9BDE4463208CC172

FASTA76488,373
        10         20         30         40         50         60 
MYTGATTYVV GFPRIGEQRE LKKVLERYWD QKTSFSEIDE IAKNLRRRHW LYQKEAGISF 

        70         80         90        100        110        120 
ISSNDFSLYD NMLDTAIMLN AVPERFSNIH DKQELYFAMA RGTNNTVAME MTKWFNTNYH 

       130        140        150        160        170        180 
YIVPELSDTM NFSLCADKII NEYREAKEYG LRTKINLIGP ITFLSLSKPV DGNQDTLELL 

       190        200        210        220        230        240 
PKILPCYVSL LKKIADLDDE VYIQFDEPIV VKDIDRRTLN LFYLCYKELS NVSNRLRLIV 

       250        260        270        280        290        300 
MTYFDHAVEA VKILSDIPIY GIGLDFVYGQ ENLKVLDSLN GKKLIAGVID GRNIWKNNYH 

       310        320        330        340        350        360 
NTLTLLKDIE KNVKKEDIIL STTCSLLHVP YSLKHENHLD KDIKSWMSFA REKLDELSDL 

       370        380        390        400        410        420 
AKLFFVENNS EDILTILENN QRIFREKQQS SKVIDPIVRE RVGNIKRRER DGSFNDRNEA 

       430        440        450        460        470        480 
QRKKLDLPLL PTTTIGSFPQ TEEIRKLRRD FKNNVISQIE YDTGIKNYID SCIQFQEDIG 

       490        500        510        520        530        540 
LDVLVHGEPE RNDMVEYFGE RLSGFVFTQN GWVQSYGSRC VKPTVIFGDV SRPKPMTIDT 

       550        560        570        580        590        600 
ILYAKSKTNK IVKGMLTGPV TILNWSYCRS DMERSAVCEQ IALAIRDEIN DLQKAGIKII 

       610        620        630        640        650        660 
QVDEAAFKEG YPLRKEKVAY YENWAVKSFK LAVSSAAIET QIHTHMCYSD FNDIIHTIEK 

       670        680        690        700        710        720 
MDADVITIET SRSGNKLLTV FATRGYKNEI GPGIYDIHSP RVPSVEELEE KIRNLMLVLP 

       730        740        750        760 
PSKLWINPDC GLKTRKWDEI RWSLSNMVKA AQHIRLGLQR VMFV 

« Hide

References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000612 Genomic DNA. Translation: ABO50276.1.
RefSeqYP_001113101.1. NC_009253.1.

3D structure databases

ProteinModelPortalA4J5C3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4J5C3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4958627.
GenomeReviewsGene locus Dred_1751 in contig CP000612_GR.
KEGGdrm:Dred_1751.
PATRIC21729693. VBIDesRed82656_1920.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0620.
HOGENOMHBG287495.
OMARNIWRAN.
PhylomeDBA4J5C3.
ProtClustDBPRK05222.

Enzyme and pathway databases

BioCycDRED349161:DRED_1751-MONOMER.

Family and domain databases

HAMAPMF_00172. Meth_synth.
[Tree]
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_DESRM
AccessionPrimary (citable) accession number: A4J5C3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2007
Last modified: January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families