Reviewed, UniProtKB/Swiss-Prot P25665 (METE_ECOLI)

Names and origin

Protein names

Recommended 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:	b3829, JW3805

Organism

Escherichia coli (strain K12) [Complete 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 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. 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
Subunit structure	Monomer. HAMAP MF_00172
Miscellaneous	Has an absolute requirement for a polyglutamylated folate as substrate. Its activity depends on phosphate anions and divalent cations. HAMAP 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
Gene Ontology (GO)
Biological process	methionine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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	1	1	Removed Ref.7
	Chain	2 – 753	752	5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172		PRO_0000098630
Regions
	Repeat	2 – 370	369	Approximate HAMAP MF_00172
	Repeat	371 – 753	383	Approximate HAMAP MF_00172
Sites
	Metal binding	641	1	Zinc HAMAP MF_00172
	Metal binding	643	1	Zinc HAMAP MF_00172
	Metal binding	726	1	Zinc HAMAP MF_00172
Experimental info
	Mutagenesis	641	1	H → N: Impaired activity, lower affinity for zinc binding. Ref.9
	Mutagenesis	641	1	H → Q: Impaired activity, lower affinity for zinc binding. Binds homocysteine 2-4x more weakly than wild-type. Ref.9
	Mutagenesis	643	1	C → S: Impaired activity, lower affinity for zinc binding. Binds homocysteine 7x tighter than wild-type. Ref.9
	Mutagenesis	726	1	C → S: Impaired activity, lower affinity for zinc binding. Binds homocysteine 2-4x more weakly than wild-type. Ref.9 Ref.8
	Sequence conflict	363	1	L → V in AAA23544. Ref.1
	Sequence conflict	605	1	E → Q in AAA67625. Ref.3
	Sequence conflict	659	1	A → R in AAA67625. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P25665-1 [UniParc]. Last modified January 23, 2007. Version 6. Checksum: C46BE52F227AFAF1	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

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: 1339288] [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: 1379743] [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: 8346018] [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: 9278503] [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: 16738553] [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: 2643109] [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: 9298646] [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: 8823155] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-726.
[9]	"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: 10625458] [Abstract] Cited for: MUTAGENESIS OF HIS-641; CYS-643 AND CYS-726.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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	AP_003971.1. NP_418273.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6847N.
IntAct	P25665. 11 interactions.
STRING	P25665.
2-D gel databases
ECO2DBASE	F088.0. 6TH EDITION.
Proteomic databases
PRIDE	P25665.
Genome annotation databases
GeneID	948323.
GenomeReviews	Gene locus JW3805 in contig AP009048_GR. Gene locus b3829 in contig U00096_GR.
KEGG	ecj:JW3805. eco:b3829.
Organism-specific databases
EchoBASE	EB0579.
EcoGene	EG10584. metE.
CMR	Search...
Phylogenomic databases
HOGENOM	P25665.
OMA	CSLLHTP.
Enzyme and pathway databases
BioCyc	EcoCyc:HOMOCYSMET-MON. MetaCyc:HOMOCYSMET-MON.
BRENDA	2.1.1.14. 246.
Gene expression databases
Genevestigator	P25665.
Family and domain databases
HAMAP	MF_00172. [Tree]
InterPro	IPR013215. Cbl-indep_Met_Synth_N. IPR002629. Methionine_synth. IPR006276. MeTrfase_B12_ind. [Graphical view]
Pfam	PF08267. Meth_synt_1. 1 hit. PF01717. Meth_synt_2. 1 hit. [Graphical view]
PIRSF	PIRSF000382. MeTrfase_B12_ind. 1 hit.
ProDom	PD004692. Methionine_synth. 1 hit. [Graphical view] [Entries sharing at least one domain]
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:	November 3, 2009
This is version 104 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)