5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

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P25665 (METE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 138. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	metE
Ordered Locus Names:	b3829, JW3805

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	753 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. HAMAP-Rule MF_00172
Sequence similarities	Belongs to the vitamin-B12 independent methionine synthase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	methionine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Inferred from direct assay PubMed 4904482. Source: EcoCyc zinc ion binding Inferred from physical interaction Ref.10. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
uvrD	P03018	1	EBI-551247,EBI-559573

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.7

Chain

2 – 753

752

5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP-Rule MF_00172

PRO_0000098630

Regions

Repeat

2 – 370

369

Approximate HAMAP-Rule MF_00172

Repeat

371 – 753

383

Approximate HAMAP-Rule MF_00172

Sites

Metal binding

641

Zinc

Metal binding

643

Zinc

Metal binding

726

Zinc

Experimental info

Mutagenesis

641

H → N: Impaired activity, lower affinity for zinc binding. Ref.10

Mutagenesis

641

H → Q: Impaired activity, lower affinity for zinc binding. Binds homocysteine 2-4x more weakly than wild-type. Ref.10

Mutagenesis

643

C → S: Impaired activity, lower affinity for zinc binding. Binds homocysteine 7x tighter than wild-type. Ref.10

Mutagenesis

726

C → S: Impaired activity, lower affinity for zinc binding. Binds homocysteine 2-4x more weakly than wild-type. Ref.8 Ref.10

Sequence conflict

363

L → V in AAA23544. Ref.1

Sequence conflict

605

E → Q in AAA67625. Ref.3

Sequence conflict

659

A → R in AAA67625. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P25665 [UniParc].

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

FASTA

753

84,674

        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' referencesShow '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 277:1453-1474(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.
PIR	A42863. F65187.
RefSeq	NP_418273.1. NC_000913.2. YP_491613.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P25665.
SMR	P25665. Positions 3-751.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6847N.
IntAct	P25665. 11 interactions.
MINT	MINT-1280694.
STRING	511145.b3829.
Proteomic databases
PaxDb	P25665.
PRIDE	P25665.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76832; AAC76832; b3829. BAE77472; BAE77472; BAE77472.
GeneID	12930483. 948323.
KEGG	ecj:Y75_p3349. eco:b3829.
PATRIC	32123159. VBIEscCol129921_3945.
Organism-specific databases
EchoBASE	EB0579.
EcoGene	EG10584. metE.
Phylogenomic databases
eggNOG	COG0620.
HOGENOM	HOG000246221.
KO	K00549.
OMA	RNIWRAN.
ProtClustDB	PRK05222.
Enzyme and pathway databases
BioCyc	EcoCyc:HOMOCYSMET-MONOMER. ECOL316407:JW3805-MONOMER. MetaCyc:HOMOCYSMET-MONOMER.
BRENDA	2.1.1.14. 2026.
UniPathway	UPA00051; UER00082.
Gene expression databases
Genevestigator	P25665.
Family and domain databases
HAMAP	MF_00172. Meth_synth.
InterPro	IPR013215. Cbl-indep_Met_Synth_N. IPR006276. Cobalamin-indep_Met_synthase. IPR002629. Methionine_synth. [Graphical view]
Pfam	PF08267. Meth_synt_1. 1 hit. PF01717. Meth_synt_2. 1 hit. [Graphical view]
PIRSF	PIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMs	TIGR01371. met_syn_B12ind. 1 hit.
ProtoNet	Search...

Entry information

Entry name

METE_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 138 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents