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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161Cobalt (cobalamin axial ligand)

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. methylaspartate mutase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. anaerobic glutamate catabolic process Source: UniProtKB-HAMAP
  2. glutamate catabolic process via L-citramalate Source: UniProtKB-UniPathway
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. Me_Asp_mutase.
[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. Me_Asp_mutase.
[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(1993) [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(1993) [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(1991) [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(1998) [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(1998) [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(2000) [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 1, 2015
This is version 90 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.