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Protein

5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

Gene

metE

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

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

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi: L-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).UniRule annotation
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 bindingi630 – 6301ZincUniRule annotation
Metal bindingi632 – 6321ZincUniRule annotation
Metal bindingi715 – 7151ZincUniRule annotation

GO - Molecular functioni

GO - Biological processi

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

BioCyciSMUT210007:GC7Z-838-MONOMER.
BRENDAi2.1.1.14. 5941.
UniPathwayiUPA00051; UER00082.

Names & Taxonomyi

Protein namesi
Recommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferaseUniRule annotation (EC:2.1.1.14UniRule annotation)
Alternative name(s):
Cobalamin-independent methionine synthaseUniRule annotation
Methionine synthase, vitamin-B12 independent isozymeUniRule annotation
Gene namesi
Name:metEUniRule annotation
Ordered Locus Names:SMU_873
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000002512 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7457455-methyltetrahydropteroyltriglutamate--homocysteine methyltransferasePRO_0000098670Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi210007.SMU_873.

Structurei

Secondary structure

1
745
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi17 – 2610Combined sources
Helixi32 – 5221Combined sources
Beta strandi56 – 616Combined sources
Helixi68 – 758Combined sources
Helixi81 – 833Combined sources
Helixi90 – 989Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi117 – 1193Combined sources
Helixi134 – 14613Combined sources
Helixi147 – 1493Combined sources
Beta strandi150 – 1556Combined sources
Helixi157 – 1626Combined sources
Helixi170 – 19021Combined sources
Beta strandi195 – 1995Combined sources
Helixi201 – 2044Combined sources
Helixi207 – 2115Combined sources
Helixi212 – 22514Combined sources
Beta strandi230 – 2345Combined sources
Helixi243 – 2464Combined sources
Beta strandi252 – 26110Combined sources
Helixi262 – 2709Combined sources
Turni271 – 2766Combined sources
Beta strandi277 – 2848Combined sources
Beta strandi286 – 2883Combined sources
Helixi294 – 30613Combined sources
Beta strandi308 – 31710Combined sources
Helixi319 – 3213Combined sources
Helixi334 – 3374Combined sources
Helixi343 – 35715Combined sources
Helixi364 – 37613Combined sources
Helixi379 – 3813Combined sources
Helixi388 – 3903Combined sources
Helixi399 – 41012Combined sources
Turni430 – 4323Combined sources
Helixi444 – 46421Combined sources
Beta strandi467 – 4693Combined sources
Helixi481 – 4844Combined sources
Beta strandi487 – 4915Combined sources
Beta strandi498 – 5014Combined sources
Beta strandi504 – 5063Combined sources
Beta strandi510 – 5178Combined sources
Helixi523 – 5319Combined sources
Beta strandi537 – 5426Combined sources
Helixi544 – 5507Combined sources
Beta strandi555 – 5573Combined sources
Helixi559 – 57921Combined sources
Beta strandi584 – 5896Combined sources
Helixi592 – 5954Combined sources
Helixi600 – 61819Combined sources
Beta strandi619 – 6213Combined sources
Beta strandi625 – 6317Combined sources
Turni637 – 6393Combined sources
Helixi640 – 6467Combined sources
Beta strandi649 – 6535Combined sources
Helixi656 – 6583Combined sources
Helixi661 – 6633Combined sources
Helixi664 – 6685Combined sources
Beta strandi674 – 6785Combined sources
Helixi690 – 6989Combined sources
Helixi699 – 7024Combined sources
Helixi706 – 7083Combined sources
Beta strandi709 – 7124Combined sources
Beta strandi717 – 7204Combined sources
Helixi722 – 74120Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NQ5X-ray1.90A2-745[»]
3L7RX-ray2.40A1-745[»]
3T0CX-ray2.19A1-745[»]
ProteinModelPortaliQ8CWX6.
SMRiQ8CWX6. Positions 1-742.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CWX6.

Family & Domainsi

Sequence similaritiesi

Belongs to the vitamin-B12 independent methionine synthase family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4107QYE. Bacteria.
COG0620. LUCA.
KOiK00549.
OMAiRFGWVQS.
OrthoDBiEOG6FFS3G.
PhylomeDBiQ8CWX6.

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.

Q8CWX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKVSSLGYP RLGENREWKK LIEAYWAGKV SKNDLFAGAK ELRLDFLKKQ
60 70 80 90 100
LNAGLDLIPV GDFSLYDHIL DLSVQFNIIP KRFAKEPIDI DLYFAIARGN
110 120 130 140 150
KENVASSMKK WFNTNYHYIV PEWSKQRPKL NNNRLLDLYL EAREVVGDKA
160 170 180 190 200
KPVITGPITY VALSTGVEDF TAAVKSLLPL YKQVFTELVK AGASYIQVDE
210 220 230 240 250
PIFVTDEGKD YLQAAKAVYA YFAKEVPDAK FIFQTYFEGL IDSQVLSQLP
260 270 280 290 300
VDAFGLDFVY GLEENLEAIK TGAFKGKEIF AGVIDGRNIW SSDFVKTSAL
310 320 330 340 350
LETIEEQSAA LTIQPSCSLL HVPVTTKNET DLDPVLRNGL AFADEKLTEV
360 370 380 390 400
KRLAEHLDGR EDPAYDLHIA HFDALQAADF RNVKLEDLSR VATKRPSDFA
410 420 430 440 450
KRRDIQQEKL HLPLLPTTTI GSFPQSREIR RTRLAWKRGD ISDAEYKQFI
460 470 480 490 500
QAEIERWIRI QEDLDLDVLV HGEFERVDMV EFFGQKLAGF TTTKFGWVQS
510 520 530 540 550
YGSRAVKPPI IYGDVQHLEP ITVEETVYAQ SLTDRPVKGM LTGPITITNW
560 570 580 590 600
SFERTDIPRD QLFNQIGLAI KDEIKLLENA GIAIIQVDEA ALREGLPLRK
610 620 630 640 650
SKQKAYLDDA VHAFHIATSS VKDETQIHTH MCYSKFDEII DAIRALDADV
660 670 680 690 700
ISIETSRSHG DIIESFETAV YPLGIGLGVY DIHSPRVPTK EEVVANIERP
710 720 730 740
LRQLSPTQFW VNPDCGLKTR QEPETIAALK VLVAATKEVR QKLGN
Length:745
Mass (Da):84,141
Last modified:March 1, 2003 - v1
Checksum:i9CD5B8905192D823
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014133 Genomic DNA. Translation: AAN58588.1.
RefSeqiNP_721282.1. NC_004350.2.
WP_002262021.1. NC_004350.2.

Genome annotation databases

EnsemblBacteriaiAAN58588; AAN58588; SMU_873.
GeneIDi1028236.
KEGGismu:SMU_873.
PATRICi19663893. VBIStrMut61772_0779.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014133 Genomic DNA. Translation: AAN58588.1.
RefSeqiNP_721282.1. NC_004350.2.
WP_002262021.1. NC_004350.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NQ5X-ray1.90A2-745[»]
3L7RX-ray2.40A1-745[»]
3T0CX-ray2.19A1-745[»]
ProteinModelPortaliQ8CWX6.
SMRiQ8CWX6. Positions 1-742.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU_873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN58588; AAN58588; SMU_873.
GeneIDi1028236.
KEGGismu:SMU_873.
PATRICi19663893. VBIStrMut61772_0779.

Phylogenomic databases

eggNOGiENOG4107QYE. Bacteria.
COG0620. LUCA.
KOiK00549.
OMAiRFGWVQS.
OrthoDBiEOG6FFS3G.
PhylomeDBiQ8CWX6.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00082.
BioCyciSMUT210007:GC7Z-838-MONOMER.
BRENDAi2.1.1.14. 5941.

Miscellaneous databases

EvolutionaryTraceiQ8CWX6.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700610 / UA159.

Entry informationi

Entry nameiMETE_STRMU
AccessioniPrimary (citable) accession number: Q8CWX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: November 11, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.