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Protein

Glutamate mutase epsilon subunit

Gene

glmE

Organism
Clostridium cochlearium
Status
Reviewed-Annotation score: Annotation score: 5 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 annotation2 Publications

Catalytic activityi

L-threo-3-methylaspartate = L-glutamate.UniRule annotation2 Publications

Cofactori

adenosylcob(III)alaminUniRule annotation4 Publications

Enzyme regulationi

Competitively inhibited by (2S,4S)-4-fluoroglutamate, 2-methyleneglutarate, (2R,3RS)-3-fluoroglutamate and (S)-3-methylitaconate.2 Publications

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. no protein annotated in this organism
  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-glutamate1
Binding sitei68Adenosylcobalamin; via carbonyl oxygen1
Binding sitei100L-glutamate1
Binding sitei123Adenosylcobalamin1
Binding sitei171L-glutamate1
Binding sitei177L-glutamate1
Binding sitei180Adenosylcobalamin; via carbonyl oxygen1
Binding sitei181L-glutamate1
Binding sitei297Adenosylcobalamin; via amide nitrogen1
Binding sitei326Adenosylcobalamin1
Binding sitei330Adenosylcobalamin; via carbonyl oxygen1
Binding sitei334Adenosylcobalamin; via amide nitrogen1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-1101.
SABIO-RKP80077.
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
OrganismiClostridium cochlearium
Taxonomic identifieri1494 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000875111 – 483Glutamate mutase epsilon subunitAdd BLAST483

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.UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
glmSP800782EBI-1028142,EBI-1028147

Protein-protein interaction databases

IntActiP80077. 1 interactor.

Structurei

Secondary structure

1483
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 20Combined sources11
Helixi21 – 23Combined sources3
Helixi25 – 29Combined sources5
Helixi32 – 40Combined sources9
Helixi44 – 46Combined sources3
Helixi48 – 58Combined sources11
Beta strandi62 – 64Combined sources3
Helixi72 – 84Combined sources13
Beta strandi89 – 95Combined sources7
Helixi99 – 101Combined sources3
Helixi104 – 117Combined sources14
Beta strandi122 – 125Combined sources4
Helixi127 – 141Combined sources15
Beta strandi146 – 149Combined sources4
Helixi156 – 164Combined sources9
Beta strandi169 – 171Combined sources3
Turni174 – 181Combined sources8
Helixi187 – 206Combined sources20
Beta strandi212 – 214Combined sources3
Turni217 – 220Combined sources4
Beta strandi221 – 223Combined sources3
Helixi226 – 242Combined sources17
Beta strandi247 – 253Combined sources7
Helixi258 – 278Combined sources21
Beta strandi285 – 291Combined sources7
Helixi301 – 318Combined sources18
Beta strandi321 – 324Combined sources4
Turni328 – 332Combined sources5
Helixi337 – 353Combined sources17
Turni354 – 356Combined sources3
Helixi363 – 386Combined sources24
Turni387 – 389Combined sources3
Helixi391 – 400Combined sources10
Beta strandi419 – 422Combined sources4
Beta strandi428 – 432Combined sources5
Helixi440 – 457Combined sources18
Helixi463 – 472Combined sources10
Turni473 – 476Combined sources4
Beta strandi477 – 479Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CB7X-ray2.00B/D1-483[»]
1CCWX-ray1.60B/D1-483[»]
1I9CX-ray1.90B/D1-483[»]
ProteinModelPortaliP80077.
SMRiP80077.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80077.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni149 – 150L-glutamate binding2

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.

P80077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELKNKKWTD EEFHKQREEV LQQWPTGKEV DLQEAVDYLK KIPAEKNFAE
60 70 80 90 100
KLVLAKKKGI TMAQPRAGVA LLDEHIELLR YLQDEGGADF LPSTIDAYTR
110 120 130 140 150
QNRYDECENG IKESEKAGRS LLNGFPGVNY GVKGCRKVLE AVNLPLQARH
160 170 180 190 200
GTPDSRLLAE IIHAGGWTSN EGGGISYNVP YAKNVTIEKS LLDWQYCDRL
210 220 230 240 250
VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA AEQGVKNITV
260 270 280 290 300
GYGECGNMIQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD
310 320 330 340 350
ESKAFGVIVT ATTIAALAGA TKVIVKTPHE AIGIPTKEAN AAGIKATKMA
360 370 380 390 400
LNMLEGQRMP MSKELETEMA VIKAETKCIL DKMFELGKGD LAIGTVKAFE
410 420 430 440 450
TGVMDIPFGP SKYNAGKMMP VRDNLGCVRY LEFGNVPFTE EIKNYNRERL
460 470 480
QERAKFEGRD VSFQMVIDDI FAVGKGRLIG RPE
Length:483
Mass (Da):53,574
Last modified:November 1, 1997 - v2
Checksum:i0789965B945B3F5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80997 Genomic DNA. Translation: CAA56923.1.
PIRiI40662.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80997 Genomic DNA. Translation: CAA56923.1.
PIRiI40662.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CB7X-ray2.00B/D1-483[»]
1CCWX-ray1.60B/D1-483[»]
1I9CX-ray1.90B/D1-483[»]
ProteinModelPortaliP80077.
SMRiP80077.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP80077. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00561; UER00617.
BioCyciMetaCyc:MONOMER-1101.
SABIO-RKP80077.

Miscellaneous databases

EvolutionaryTraceiP80077.

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_CLOCO
AccessioniPrimary (citable) accession number: P80077
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.