Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P25665 (METE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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:
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:b3829, JW3805
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. HAMAP-Rule MF_00172

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit.

Pathway

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

Subunit structure

Monomer.

Miscellaneous

Has an absolute requirement for a polyglutamylated folate as substrate. Its activity depends on phosphate anions and divalent cations.

Sequence similarities

Belongs to the vitamin-B12 independent methionine synthase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

uvrDP030182EBI-551247,EBI-559573

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 7537525-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP-Rule MF_00172
PRO_0000098630

Regions

Repeat2 – 370369Approximate HAMAP-Rule MF_00172
Repeat371 – 753383Approximate HAMAP-Rule MF_00172

Sites

Metal binding6411Zinc
Metal binding6431Zinc
Metal binding7261Zinc

Experimental info

Mutagenesis6411H → N: Impaired activity, lower affinity for zinc binding. Ref.10
Mutagenesis6411H → Q: Impaired activity, lower affinity for zinc binding. Binds homocysteine 2-4x more weakly than wild-type. Ref.10
Mutagenesis6431C → S: Impaired activity, lower affinity for zinc binding. Binds homocysteine 7x tighter than wild-type. Ref.10
Mutagenesis7261C → S: Impaired activity, lower affinity for zinc binding. Binds homocysteine 2-4x more weakly than wild-type. Ref.8 Ref.10
Sequence conflict3631L → V in AAA23544. Ref.1
Sequence conflict6051E → Q in AAA67625. Ref.3
Sequence conflict6591A → R in AAA67625. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P25665 [UniParc].

Last modified January 23, 2007. Version 6.
Checksum: C46BE52F227AFAF1

FASTA75384,674
        10         20         30         40         50         60 
MTILNHTLGF PRVGLRRELK KAQESYWAGN STREELLAVG RELRARHWDQ QKQAGIDLLP 

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

       130        140        150        160        170        180 
TNYHYMVPEF VKGQQFKLTW TQLLDEVDEA LALGHKVKPV LLGPVTWLWL 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 IAEHIKQAIV 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

« Hide 'large scale' references
[1]"Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: two solutions to the same chemical problem."
Gonzalez J.C., Banerjee R.V., Huang S., Sumner J.S., Matthews R.G.
Biochemistry 31:6045-6056(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: K12 / DH5-alpha.
[2]"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 604 AND 658.
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Regulation of methionine synthesis in Escherichia coli: effect of the MetR protein on the expression of the metE and metR genes."
Maxon M.E., Redfield B., Cai X.-Y., Shoeman R., Fujita K., Fisher W., Stauffer G., Weissbach H., Brot N.
Proc. Natl. Acad. Sci. U.S.A. 86:85-89(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[8]"Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme."
Gonzalez J.C., Peariso K., Penner-Hahn J.E., Matthews R.G.
Biochemistry 35:12228-12234(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-726.
[9]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[10]"Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli."
Zhou Z.S., Peariso K., Penner-Hahn J.E., Matthews R.G.
Biochemistry 38:15915-15926(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-641; CYS-643 AND CYS-726.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87625 Genomic DNA. Translation: AAA23544.1.
M87049 Genomic DNA. Translation: AAA67625.1.
U00096 Genomic DNA. Translation: AAC76832.1.
AP009048 Genomic DNA. Translation: BAE77472.1.
J04155 Genomic DNA. Translation: AAA24160.1.
PIRA42863. F65187.
RefSeqNP_418273.1. NC_000913.3.
YP_491613.1. NC_007779.1.

3D structure databases

ProteinModelPortalP25665.
SMRP25665. Positions 3-751.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6847N.
IntActP25665. 11 interactions.
MINTMINT-1280694.
STRING511145.b3829.

Proteomic databases

PaxDbP25665.
PRIDEP25665.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76832; AAC76832; b3829.
BAE77472; BAE77472; BAE77472.
GeneID12930483.
948323.
KEGGecj:Y75_p3349.
eco:b3829.
PATRIC32123159. VBIEscCol129921_3945.

Organism-specific databases

EchoBASEEB0579.
EcoGeneEG10584. metE.

Phylogenomic databases

eggNOGCOG0620.
HOGENOMHOG000246221.
KOK00549.
OMAFKANPAH.
OrthoDBEOG6FFS3G.
PhylomeDBP25665.

Enzyme and pathway databases

BioCycEcoCyc:HOMOCYSMET-MONOMER.
ECOL316407:JW3805-MONOMER.
MetaCyc:HOMOCYSMET-MONOMER.
BRENDA2.1.1.14. 2026.
UniPathwayUPA00051; UER00082.

Gene expression databases

GenevestigatorP25665.

Family and domain databases

HAMAPMF_00172. Meth_synth.
InterProIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Met_Synth_C/arc.
[Graphical view]
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...

Other

PROP25665.

Entry information

Entry nameMETE_ECOLI
AccessionPrimary (citable) accession number: P25665
Secondary accession number(s): Q2M8D4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 146 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene