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Protein

5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

Gene

metE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Pathway:iL-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-methionine from L-homocysteine (MetE route).
Proteins known to be involved in this subpathway in this organism are:
  1. 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (metE)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from L-homocysteine (MetE route), the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi641 – 6411Zinc
Metal bindingi643 – 6431Zinc
Metal bindingi726 – 7261Zinc

GO - Molecular functioni

  • 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Source: EcoCyc
  • methionine synthase activity Source: BHF-UCL
  • protein methyltransferase activity Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • homocysteine metabolic process Source: BHF-UCL
  • methionine biosynthetic process Source: BHF-UCL
  • protein methylation Source: GOC
  • tetrahydrofolate interconversion Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:HOMOCYSMET-MONOMER.
ECOL316407:JW3805-MONOMER.
MetaCyc:HOMOCYSMET-MONOMER.
BRENDAi2.1.1.14. 2026.
UniPathwayiUPA00051; UER00082.

Names & Taxonomyi

Protein namesi
Recommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC:2.1.1.14)
Alternative name(s):
Cobalamin-independent methionine synthase
Methionine synthase, vitamin-B12 independent isozyme
Gene namesi
Name:metE
Ordered Locus Names:b3829, JW3805
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10584. metE.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi641 – 6411H → N: Impaired activity, lower affinity for zinc binding. 1 Publication
Mutagenesisi641 – 6411H → Q: Impaired activity, lower affinity for zinc binding. Binds homocysteine 2-4x more weakly than wild-type. 1 Publication
Mutagenesisi643 – 6431C → S: Impaired activity, lower affinity for zinc binding. Binds homocysteine 7x tighter than wild-type. 1 Publication
Mutagenesisi726 – 7261C → S: Impaired activity, lower affinity for zinc binding. Binds homocysteine 2-4x more weakly than wild-type. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 7537525-methyltetrahydropteroyltriglutamate--homocysteine methyltransferasePRO_0000098630Add
BLAST

Proteomic databases

PaxDbiP25665.
PRIDEiP25665.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
uvrDP030182EBI-551247,EBI-559573

Protein-protein interaction databases

DIPiDIP-6847N.
IntActiP25665. 11 interactions.
MINTiMINT-1280694.
STRINGi511145.b3829.

Structurei

3D structure databases

ProteinModelPortaliP25665.
SMRiP25665. Positions 3-751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati2 – 370369ApproximateAdd
BLAST
Repeati371 – 753383ApproximateAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0620.
HOGENOMiHOG000246221.
InParanoidiP25665.
KOiK00549.
OMAiRFGWVQS.
OrthoDBiEOG6FFS3G.
PhylomeDBiP25665.

Family and domain databases

HAMAPiMF_00172. Meth_synth.
InterProiIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Met_Synth_C/arc.
[Graphical view]
PfamiPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMsiTIGR01371. met_syn_B12ind. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25665-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTILNHTLGF PRVGLRRELK KAQESYWAGN STREELLAVG RELRARHWDQ
60 70 80 90 100
QKQAGIDLLP VGDFAWYDHV LTTSLLLGNV PARHQNKDGS VDIDTLFRIG
110 120 130 140 150
RGRAPTGEPA AAAEMTKWFN TNYHYMVPEF VKGQQFKLTW TQLLDEVDEA
160 170 180 190 200
LALGHKVKPV LLGPVTWLWL GKVKGEQFDR LSLLNDILPV YQQVLAELAK
210 220 230 240 250
RGIEWVQIDE PALVLELPQA WLDAYKPAYD ALQGQVKLLL TTYFEGVTPN
260 270 280 290 300
LDTITALPVQ GLHVDLVHGK DDVAELHKRL PSDWLLSAGL INGRNVWRAD
310 320 330 340 350
LTEKYAQIKD IVGKRDLWVA SSCSLLHSPI DLSVETRLDA EVKSWFAFAL
360 370 380 390 400
QKCHELALLR DALNSGDTAA LAEWSAPIQA RRHSTRVHNP AVEKRLAAIT
410 420 430 440 450
AQDSQRANVY EVRAEAQRAR FKLPAWPTTT IGSFPQTTEI RTLRLDFKKG
460 470 480 490 500
NLDANNYRTG IAEHIKQAIV EQERLGLDVL VHGEAERNDM VEYFGEHLDG
510 520 530 540 550
FVFTQNGWVQ SYGSRCVKPP IVIGDISRPA PITVEWAKYA QSLTDKPVKG
560 570 580 590 600
MLTGPVTILC WSFPREDVSR ETIAKQIALA LRDEVADLEA AGIGIIQIDE
610 620 630 640 650
PALREGLPLR RSDWDAYLQW GVEAFRINAA VAKDDTQIHT HMCYCEFNDI
660 670 680 690 700
MDSIAALDAD VITIETSRSD MELLESFEEF DYPNEIGPGV YDIHSPNVPS
710 720 730 740 750
VEWIEALLKK AAKRIPAERL WVNPDCGLKT RGWPETRAAL ANMVQAAQNL

RRG
Length:753
Mass (Da):84,674
Last modified:January 23, 2007 - v6
Checksum:iC46BE52F227AFAF1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti363 – 3631L → V in AAA23544 (PubMed:1339288).Curated
Sequence conflicti605 – 6051E → Q in AAA67625 (PubMed:8346018).Curated
Sequence conflicti659 – 6591A → R in AAA67625 (PubMed:8346018).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF65187. A42863.
RefSeqiNP_418273.1. NC_000913.3.
WP_000153907.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76832; AAC76832; b3829.
BAE77472; BAE77472; BAE77472.
GeneIDi948323.
KEGGieco:b3829.
PATRICi32123159. VBIEscCol129921_3945.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF65187. A42863.
RefSeqiNP_418273.1. NC_000913.3.
WP_000153907.1. NZ_CP010445.1.

3D structure databases

ProteinModelPortaliP25665.
SMRiP25665. Positions 3-751.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6847N.
IntActiP25665. 11 interactions.
MINTiMINT-1280694.
STRINGi511145.b3829.

Proteomic databases

PaxDbiP25665.
PRIDEiP25665.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76832; AAC76832; b3829.
BAE77472; BAE77472; BAE77472.
GeneIDi948323.
KEGGieco:b3829.
PATRICi32123159. VBIEscCol129921_3945.

Organism-specific databases

EchoBASEiEB0579.
EcoGeneiEG10584. metE.

Phylogenomic databases

eggNOGiCOG0620.
HOGENOMiHOG000246221.
InParanoidiP25665.
KOiK00549.
OMAiRFGWVQS.
OrthoDBiEOG6FFS3G.
PhylomeDBiP25665.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00082.
BioCyciEcoCyc:HOMOCYSMET-MONOMER.
ECOL316407:JW3805-MONOMER.
MetaCyc:HOMOCYSMET-MONOMER.
BRENDAi2.1.1.14. 2026.

Miscellaneous databases

PROiP25665.

Family and domain databases

HAMAPiMF_00172. Meth_synth.
InterProiIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Met_Synth_C/arc.
[Graphical view]
PfamiPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMsiTIGR01371. met_syn_B12ind. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiMETE_ECOLI
AccessioniPrimary (citable) accession number: P25665
Secondary accession number(s): Q2M8D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 154 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.