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Reviewed, UniProtKB/Swiss-Prot A7ZU36 (METE_ECO24)

Last modified November 3, 2009. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
    EC=2.1.1.14
Alternative name(s):
    Methionine synthase, vitamin-B12 independent isozyme
    Cobalamin-independent methionine synthase
Gene names
Name: metE
Ordered Locus Names: EcE24377A_4350
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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 – 7537535-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172
PRO_1000058313

Sites

Metal binding6411Zinc By similarity
Metal binding6431Zinc By similarity
Metal binding7261Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZU36-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 781FCD54F7C4C990

FASTA75384,735
        10         20         30         40         50         60 
MTILNHTLGF PRVGLRRELK KAQESYWAGN STREELLTVG RELRARHWDQ QKQAGIDLLP 

        70         80         90        100        110        120 
VGDFAWYDHV LTTSLLLGNV PPRHQNKDGS VDIDTLFRIG RGRAPTGEPA AAAEMTKWFN 

       130        140        150        160        170        180 
TNYHYMVPEF VKGQQFKLTW TQLLEEVDEA LALGHNVKPV LLGPVTYLWL GKVKGEQFDR 

       190        200        210        220        230        240 
LSLLNDILPV YQQVLAELAK RGIEWVQIDE PALVLELPQA WLDAYKPAYD ALQGQVKLLL 

       250        260        270        280        290        300 
TTYFEGVTPN LDTITALPVQ GLHVDLVHGK DDVAELHKRL PSDWLLSAGL INGRNVWRAD 

       310        320        330        340        350        360 
LTEKYAQIKD IVGKRDLWVA SSCSLLHSPI DLSVETRLDA EVKSWFAFAL QKCHELALLR 

       370        380        390        400        410        420 
DALNSGDTAA LAEWSAPIQA RRHSTRVHNP AVEKRLAAIT AQDSQRANVY EVRAEAQRAR 

       430        440        450        460        470        480 
FKLPAWPTTT IGSFPQTTEI RTLRLDFKKG NLDANNYRTG IAEHIRQAIV EQERLGLDVL 

       490        500        510        520        530        540 
VHGEAERNDM VEYFGEHLDG FVFTQNGWVQ SYGSRCVKPP IVIGDISRPA PITVEWAKYA 

       550        560        570        580        590        600 
QSLTDKPVKG MLTGPVTILC WSFPREDVSR ETIAKQIALA LRDEVADLEA AGIGIIQIDE 

       610        620        630        640        650        660 
PALREGLPLR RSDWDAYLQW GVEAFRINAA VAKDDTQIHT HMCYCEFNDI MDSIAALDAD 

       670        680        690        700        710        720 
VITIETSRSD MELLESFEEF DYPNEIGPGV YDIHSPNVPS VEWIEALLKK AAKRIPAERL 

       730        740        750 
WVNPDCGLKT RGWPETRAAL ANMVQAAQNL RRG 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000800 Genomic DNA. Translation: ABV19772.1.
RefSeqYP_001465315.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZU36.

Genome annotation databases

GeneID5589931.
GenomeReviewsGene locus EcE24377A_4350 in contig CP000800_GR.
KEGGecw:EcE24377A_4350.
NMPDRfig|331111.3.peg.1976.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMACSLLHTP.

Family and domain databases

HAMAPMF_00172.
[Tree]
InterProIPR013215. Cbl-indep_Met_Synth_N.
IPR002629. Methionine_synth.
IPR006276. MeTrfase_B12_ind.
[Graphical view]
PfamPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFPIRSF000382. MeTrfase_B12_ind. 1 hit.
ProDomPD004692. Methionine_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01371. met_syn_B12ind. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMETE_ECO24
AccessionPrimary (citable) accession number: A7ZU36
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: November 3, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents