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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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161Cobalt (cobalamin axial ligand)

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Glutamate mutase sigma subunitPRO_0000216443Add
BLAST

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 interaction.

Structurei

Secondary structure

1
137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Helixi18 – 2912Combined sources
Beta strandi33 – 419Combined sources
Helixi43 – 5311Combined sources
Beta strandi56 – 627Combined sources
Helixi67 – 715Combined sources
Helixi74 – 807Combined sources
Beta strandi87 – 937Combined sources
Beta strandi95 – 984Combined sources
Helixi101 – 11010Combined sources
Beta strandi114 – 1163Combined sources
Helixi123 – 13412Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP80078.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 137135B12-bindingUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 175Adenosylcobalamin binding
Regioni61 – 633Adenosylcobalamin binding
Regioni93 – 975Adenosylcobalamin binding

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.40.50.280. 1 hit.
HAMAPiMF_00526. Me_Asp_mutase_S.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1ANMR-A1-137[»]
1CB7X-ray2.00A/C1-137[»]
1CCWX-ray1.60A/C1-137[»]
1I9CX-ray1.90A/C1-137[»]
ProteinModelPortaliP80078.
SMRiP80078. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP80078. 1 interaction.

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

Gene3Di3.40.50.280. 1 hit.
HAMAPiMF_00526. Me_Asp_mutase_S.
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...

Publicationsi

  1. "Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli."
    Zelder O., Beatrix B., Leutbecher U., Buckel W.
    Eur. J. Biochem. 226:577-585(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, SUBUNIT.
    Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
  2. "Cloning, sequencing and expression in Escherichia coli of the gene encoding component S of the coenzyme B12-dependent glutamate mutase from Clostridium cochlearium."
    Zelder O., Beatrix B., Buckel W.
    FEMS Microbiol. Lett. 118:15-21(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
    Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
  3. "Glutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors."
    Leutbecher U., Boecher R., Linder D., Buckel W.
    Eur. J. Biochem. 205:759-765(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-23, FUNCTION, ENZYME REGULATION, COFACTOR, SUBUNIT.
    Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
  4. "Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium."
    Hoffmann B., Konrat R., Bothe H., Buckel W., Krautler B.
    Eur. J. Biochem. 263:178-188(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  5. "Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights."
    Reitzer R., Gruber K., Jogl G., Wagner U.G., Bothe H., Buckel W., Kratky C.
    Structure 7:891-902(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS, COFACTOR, SUBUNIT.
    Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
  6. "Radical shuttling in a protein: ribose pseudorotation controls alkyl-radical transfer in the coenzyme B(12) dependent enzyme glutamate mutase."
    Gruber K., Reitzer R., Kratky C.
    Angew. Chem. Int. Ed. Engl. 40:3377-3380(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS AND SUBSTRATE, COFACTOR, SUBUNIT.

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: April 29, 2015
This is version 91 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

External Data

Dasty 3

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 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.