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Protein

Glutamate mutase sigma subunit

Gene

glmS

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 annotation3 Publications

Catalytic activityi

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

Cofactori

adenosylcob(III)alaminUniRule annotation5 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
Metal bindingi16Cobalt (cobalamin axial ligand)1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

BRENDAi5.4.99.1. 1471.
SABIO-RKP80078.
UniPathwayiUPA00561; UER00617.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate mutase sigma subunitUniRule annotation (EC:5.4.99.1UniRule annotation)
Alternative name(s):
Glutamate mutase S chainUniRule annotation
Glutamate mutase small subunitUniRule annotation
Methylaspartate mutaseUniRule annotation
Gene namesi
Name:glmSUniRule annotation
OrganismiClostridium cochlearium
Taxonomic identifieri1494 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002164431 – 137Glutamate mutase sigma subunitAdd BLAST137

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 annotation5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
glmEP800772EBI-1028147,EBI-1028142

Protein-protein interaction databases

IntActiP80078. 1 interactor.

Structurei

Secondary structure

1137
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Helixi18 – 29Combined sources12
Beta strandi33 – 41Combined sources9
Helixi43 – 53Combined sources11
Beta strandi56 – 62Combined sources7
Helixi67 – 71Combined sources5
Helixi74 – 80Combined sources7
Beta strandi87 – 93Combined sources7
Beta strandi95 – 98Combined sources4
Helixi101 – 110Combined sources10
Beta strandi114 – 116Combined sources3
Helixi123 – 134Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B1ANMR-A1-137[»]
1CB7X-ray2.00A/C1-137[»]
1CCWX-ray1.60A/C1-137[»]
1I9CX-ray1.90A/C1-137[»]
ProteinModelPortaliP80078.
SMRiP80078.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80078.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 137B12-bindingUniRule annotationAdd BLAST135

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 17Adenosylcobalamin binding5
Regioni61 – 63Adenosylcobalamin binding3
Regioni93 – 97Adenosylcobalamin binding5

Sequence similaritiesi

Belongs to the methylaspartate mutase GlmS subunit family.UniRule annotation
Contains 1 B12-binding domain.UniRule annotation

Family and domain databases

CDDicd02072. Glm_B12_BD. 1 hit.
Gene3Di3.40.50.280. 1 hit.
HAMAPiMF_00526. Me_Asp_mutase_S. 1 hit.
InterProiIPR006158. Cobalamin-bd.
IPR006394. GlmS.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR01501. MthylAspMutase. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80078-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKKTIVLGV IGSDCHAVGN KILDHAFTNA GFNVVNIGVL SPQEVFIKAA
60 70 80 90 100
IETKADAILL SSLYGQGEID CKGLRQKCDE AGLEGILLYV GGNIVVGKQH
110 120 130
WPDVEKRFKD MGYDRVYAPG TPPEVGIADL KKDLNIE
Length:137
Mass (Da):14,812
Last modified:December 13, 2001 - v2
Checksum:iD9C5BF8DE5D1E878
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80997 Genomic DNA. Translation: CAA56921.1.
X75890 Genomic DNA. Translation: CAA53484.1.
PIRiI40658.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80997 Genomic DNA. Translation: CAA56921.1.
X75890 Genomic DNA. Translation: CAA53484.1.
PIRiI40658.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B1ANMR-A1-137[»]
1CB7X-ray2.00A/C1-137[»]
1CCWX-ray1.60A/C1-137[»]
1I9CX-ray1.90A/C1-137[»]
ProteinModelPortaliP80078.
SMRiP80078.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP80078. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00561; UER00617.
BRENDAi5.4.99.1. 1471.
SABIO-RKP80078.

Miscellaneous databases

EvolutionaryTraceiP80078.

Family and domain databases

CDDicd02072. Glm_B12_BD. 1 hit.
Gene3Di3.40.50.280. 1 hit.
HAMAPiMF_00526. Me_Asp_mutase_S. 1 hit.
InterProiIPR006158. Cobalamin-bd.
IPR006394. GlmS.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR01501. MthylAspMutase. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGMSS_CLOCO
AccessioniPrimary (citable) accession number: P80078
Secondary accession number(s): Q60144
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 13, 2001
Last modified: November 2, 2016
This is version 95 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.