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Protein

Glutamate mutase epsilon subunit

Gene

glmE

Organism
Clostridium tetanomorphum
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).UniRule annotation1 Publication

Catalytic activityi

L-threo-3-methylaspartate = L-glutamate.UniRule annotation1 Publication

Cofactori

adenosylcob(III)alaminUniRule annotation1 Publication

Kineticsi

Kcat is 20.6 sec(-1) for mutase activity with L-glutamate.

  1. KM=18 µM for adenosylcobalamin1 Publication
  2. KM=1.09 mM for L-glutamate1 Publication
  1. Vmax=22.8 µmol/min/mg enzyme1 Publication

Pathwayi: L-glutamate degradation via mesaconate pathway

This protein is involved in step 1 of the subpathway that synthesizes acetate and pyruvate from L-glutamate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Glutamate mutase sigma subunit (glmS), Glutamate mutase epsilon subunit (glmE)
  2. Methylaspartate ammonia-lyase
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway L-glutamate degradation via mesaconate pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetate and pyruvate from L-glutamate, the pathway L-glutamate degradation via mesaconate pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei66L-glutamateUniRule annotation1
Binding sitei68Adenosylcobalamin; via carbonyl oxygenUniRule annotation1
Binding sitei100L-glutamateUniRule annotation1
Binding sitei123AdenosylcobalaminUniRule annotation1
Binding sitei171L-glutamateUniRule annotation1
Binding sitei177L-glutamateUniRule annotation1
Binding sitei180Adenosylcobalamin; via carbonyl oxygenUniRule annotation1
Binding sitei181L-glutamateUniRule annotation1
Binding sitei297Adenosylcobalamin; via amide nitrogenUniRule annotation1
Binding sitei326AdenosylcobalaminUniRule annotation1
Binding sitei330Adenosylcobalamin; via carbonyl oxygenUniRule annotation1
Binding sitei334Adenosylcobalamin; via amide nitrogenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt

Enzyme and pathway databases

SABIO-RKQ05509.
UniPathwayiUPA00561; UER00617.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate mutase epsilon subunitUniRule annotation (EC:5.4.99.1UniRule annotation)
Alternative name(s):
Glutamate mutase E chainUniRule annotation
Glutamate mutase large subunitUniRule annotation
Methylaspartate mutaseUniRule annotation
Gene namesi
Name:glmEUniRule annotation
Synonyms:mutE
OrganismiClostridium tetanomorphum
Taxonomic identifieri1553 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000875121 – 485Glutamate mutase epsilon subunitAdd BLAST485

Interactioni

Subunit structurei

Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer (Probable).1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ05509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni149 – 150L-glutamate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the methylaspartate mutase GlmE subunit family.UniRule annotation

Family and domain databases

CDDicd00245. Glm_e. 1 hit.
Gene3Di3.20.20.240. 1 hit.
3.90.970.10. 1 hit.
HAMAPiMF_01923. Me_Asp_mutase_E. 1 hit.
InterProiIPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006396. Glu_mut_E.
IPR014714. Glu_mut_E_C_dom.
[Graphical view]
PfamiPF06368. Met_asp_mut_E. 1 hit.
[Graphical view]
PIRSFiPIRSF001495. Met_asp_mut_epsi. 1 hit.
SUPFAMiSSF51703. SSF51703. 1 hit.
TIGRFAMsiTIGR01503. MthylAspMut_E. 1 hit.

Sequencei

Sequence statusi: Complete.

Q05509-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELKNKKWTD EEFFKQREEV LKQWPTGKEV DLQEAVDYLK KVPTEKNFAD
60 70 80 90 100
KLVRAKEAGI TLAQPRAGVA LLDEHINLLR YLQDEGGADL LPSTIDAYTR
110 120 130 140 150
QNRYEECEIG IKESEKAGRS LLNGFPGVNH GVKGCRKVLE SVNLPLQARH
160 170 180 190 200
GTPDSRLLAE IIHAGGWTSN EGGGISYNIP YAKSVPIDKC LKDWQYCDRL
210 220 230 240 250
VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA AEQGVKNITV
260 270 280 290 300
GYGECGNMLQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD
310 320 330 340 350
ESKAFGVIVT ATTIASLAGA TKVIVKTPHE AIGIPTKEAN ASGIKATKMA
360 370 380 390 400
LNMLEGQRMP MSKELETEMA IIKAETKCIL DKMFELGKGD LAVGTVKAFE
410 420 430 440 450
TGVMDIPFGP SKYNAGKMMP VRDNLGCVRY LEFGNVPFTE ELKNYNRERL
460 470 480
AERAKFEGRE VSFQMVIDDI FAVGKGRLIG RPENK
Length:485
Mass (Da):53,741
Last modified:February 1, 1995 - v1
Checksum:i131792A392CACCC0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8W → L AA sequence (PubMed:1397267).Curated1
Sequence conflicti12E → G AA sequence (PubMed:1397267).Curated1
Sequence conflicti17R → A AA sequence (PubMed:1397267).Curated1
Sequence conflicti19E → G AA sequence (PubMed:1397267).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70499 Genomic DNA. Translation: CAA49910.1.
X70695 Genomic DNA. Translation: CAA50026.1.
S48141 Genomic DNA. Translation: AAB24069.1.
PIRiS32433.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70499 Genomic DNA. Translation: CAA49910.1.
X70695 Genomic DNA. Translation: CAA50026.1.
S48141 Genomic DNA. Translation: AAB24069.1.
PIRiS32433.

3D structure databases

ProteinModelPortaliQ05509.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00561; UER00617.
SABIO-RKQ05509.

Family and domain databases

CDDicd00245. Glm_e. 1 hit.
Gene3Di3.20.20.240. 1 hit.
3.90.970.10. 1 hit.
HAMAPiMF_01923. Me_Asp_mutase_E. 1 hit.
InterProiIPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006396. Glu_mut_E.
IPR014714. Glu_mut_E_C_dom.
[Graphical view]
PfamiPF06368. Met_asp_mut_E. 1 hit.
[Graphical view]
PIRSFiPIRSF001495. Met_asp_mut_epsi. 1 hit.
SUPFAMiSSF51703. SSF51703. 1 hit.
TIGRFAMsiTIGR01503. MthylAspMut_E. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLME_CLOTT
AccessioniPrimary (citable) accession number: Q05509
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 5, 2016
This is version 77 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

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.