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Q05488

- GMSS_CLOTT

UniProt

Q05488 - GMSS_CLOTT

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Protein
Glutamate mutase sigma subunit
Gene
glmS, mutS
Organism
Clostridium tetanomorphum
Status
Reviewed - 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).1 Publication

Catalytic activityi

L-threo-3-methylaspartate = L-glutamate.1 Publication

Cofactori

Adenosylcobalamin.1 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-glutamate

Vmax=22.8 µmol/min/mg enzyme

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 subunit (EC:5.4.99.1)
Alternative name(s):
Glutamate mutase S chain
Glutamate mutase small subunit
Methylaspartate mutase
Gene namesi
Name:glmS
Synonyms:mutS
OrganismiClostridium tetanomorphum
Taxonomic identifieri1553 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Glutamate mutase sigma subunitUniRule annotation
PRO_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.1 Publication

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE1NMR-A1-137[»]
1FMFNMR-A1-137[»]
1ID8NMR-A1-137[»]
ProteinModelPortaliQ05488.
SMRiQ05488. Positions 1-137.

Miscellaneous databases

EvolutionaryTraceiQ05488.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 137135B12-binding
Add
BLAST

Region

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

Sequence similaritiesi

Contains 1 B12-binding domain.

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

MEKKTIVLGV IGSDCHAVGN KILDHSFTNA GFNVVNIGVL SSQEDFINAA    50
IETKADLICV SSLYGQGEID CKGLREKCDE AGLKGIKLFV GGNIVVGKQN 100
WPDVEQRFKA MGFDRVYPPG TSPETTIADM KEVLGVE 137
Length:137
Mass (Da):14,748
Last modified:February 1, 1995 - v1
Checksum:iE71FE55BA8CE3DB3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X70499 Genomic DNA. Translation: CAA49908.1.
X68570 Genomic DNA. Translation: CAA48567.1.
PIRiS29502.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X70499 Genomic DNA. Translation: CAA49908.1 .
X68570 Genomic DNA. Translation: CAA48567.1 .
PIRi S29502.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BE1 NMR - A 1-137 [» ]
1FMF NMR - A 1-137 [» ]
1ID8 NMR - A 1-137 [» ]
ProteinModelPortali Q05488.
SMRi Q05488. Positions 1-137.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00561 ; UER00617 .
SABIO-RK Q05488.

Miscellaneous databases

EvolutionaryTracei Q05488.

Family and domain databases

Gene3Di 3.40.50.280. 1 hit.
HAMAPi MF_00526. Me_Asp_mutase_S.
InterProi IPR006158. Cobalamin-bd.
IPR006394. Me_Asp_mutase.
[Graphical view ]
Pfami PF02310. B12-binding. 1 hit.
[Graphical view ]
SUPFAMi SSF52242. SSF52242. 1 hit.
TIGRFAMsi TIGR01501. MthylAspMutase. 1 hit.
PROSITEi PS51332. B12_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 80 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

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