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Protein

Glutamate mutase sigma subunit

Gene

glmS

Organism
Clostridium tetanomorphum
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 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

Vmax=22.8 µmol/min/mg enzyme1 Publication

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

SABIO-RKQ05488.
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
Synonyms:mutS
OrganismiClostridium tetanomorphum
Taxonomic identifieri1553 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Glutamate mutase sigma subunitPRO_0000216445Add
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 annotation1 Publication

Structurei

Secondary structure

1
137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Beta strandi13 – 164Combined sources
Beta strandi20 – 223Combined sources
Beta strandi25 – 284Combined sources
Turni29 – 313Combined sources
Beta strandi33 – 408Combined sources
Helixi45 – 528Combined sources
Beta strandi56 – 6611Combined sources
Helixi67 – 715Combined sources
Helixi75 – 784Combined sources
Beta strandi87 – 926Combined sources
Beta strandi94 – 963Combined sources
Helixi104 – 1118Combined sources
Beta strandi114 – 1163Combined sources
Turni123 – 1286Combined sources
Helixi129 – 1324Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE1NMR-A1-137[»]
1FMFNMR-A1-137[»]
1ID8NMR-A1-137[»]
ProteinModelPortaliQ05488.
SMRiQ05488. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05488.

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 bindingUniRule annotation
Regioni61 – 633Adenosylcobalamin bindingUniRule annotation
Regioni93 – 975Adenosylcobalamin bindingUniRule annotation

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.

Q05488-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKKTIVLGV IGSDCHAVGN KILDHSFTNA GFNVVNIGVL SSQEDFINAA
60 70 80 90 100
IETKADLICV SSLYGQGEID CKGLREKCDE AGLKGIKLFV GGNIVVGKQN
110 120 130
WPDVEQRFKA MGFDRVYPPG TSPETTIADM KEVLGVE
Length:137
Mass (Da):14,748
Last modified:February 1, 1995 - v1
Checksum:iE71FE55BA8CE3DB3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70499 Genomic DNA. Translation: CAA49908.1.
X68570 Genomic DNA. Translation: CAA48567.1.
PIRiS29502.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70499 Genomic DNA. Translation: CAA49908.1.
X68570 Genomic DNA. Translation: CAA48567.1.
PIRiS29502.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE1NMR-A1-137[»]
1FMFNMR-A1-137[»]
1ID8NMR-A1-137[»]
ProteinModelPortaliQ05488.
SMRiQ05488. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00561; UER00617.
SABIO-RKQ05488.

Miscellaneous databases

EvolutionaryTraceiQ05488.

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. "Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes."
    Marsh E.N.G., Holloway D.E.
    FEBS Lett. 310:167-170(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-33.
    Strain: NCIMB 11547.
  2. "Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum."
    Brecht M., Kellermann J., Plueckthun A.
    FEBS Lett. 319:84-89(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-24.
    Strain: ATCC 15920 / DSM 528 / H1.
  3. "Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme."
    Holloway D.E., Marsh E.N.
    J. Biol. Chem. 269:20425-20430(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
  4. "How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum."
    Tollinger M., Konrat R., Hilbert B.H., Marsh E.N.G., Kraeutler B.
    Structure 6:1021-1033(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
    Strain: ATCC 15920 / DSM 528 / H1.
  5. "A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum."
    Hoffmann B., Tollinger M., Konrat R., Huhta M., Marsh E.N., Krautler B.
    ChemBioChem 2:643-655(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  6. "The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12)."
    Tollinger M., Eichmuller C., Konrat R., Huhta M.S., Marsh E.N., Krautler B.
    J. Mol. Biol. 309:777-791(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiGMSS_CLOTT
AccessioniPrimary (citable) accession number: Q05488
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 82 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

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.