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Protein

Glutamate mutase sigma subunit

Gene

glmS

Organism
Desulfitobacterium hafniense (strain Y51)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).UniRule annotation

Catalytic activityi

L-threo-3-methylaspartate = L-glutamate.UniRule annotation

Cofactori

adenosylcob(III)alaminUniRule annotation

Pathwayi

Sites

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

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

BioCyciDHAF138119:GHT5-3308-MONOMER.
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:mamA
Ordered Locus Names:DSY3236
OrganismiDesulfitobacterium hafniense (strain Y51)
Taxonomic identifieri138119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium
ProteomesiUP000001946 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 136136Glutamate mutase sigma subunitPRO_0000264142Add
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 annotation

Protein-protein interaction databases

STRINGi138119.DSY3236.

Structurei

3D structure databases

SMRiQ24SG7. Positions 1-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 136134B12-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

Phylogenomic databases

eggNOGiCOG2185.
HOGENOMiHOG000011065.
KOiK01846.
OMAiGHGEMDC.
OrthoDBiEOG6CP428.

Family and domain databases

Gene3Di3.40.50.280. 1 hit.
HAMAPiMF_00526. Me_Asp_mutase_S.
InterProiIPR006159. Acid_CoA_mut_C.
IPR006158. Cobalamin-bd.
IPR006394. GlmS.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR01501. MthylAspMutase. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q24SG7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGKTLVLGV IGADVHAVGN RILDYAFTQA GFKVINIGVL ASQEEFIRAA
60 70 80 90 100
IETAASVIMV SSLYGHGELD CRGLREKCQE SGIGDILLYV GGNLVVGKQE
110 120 130
FSEVEKRFLA MGFNRVYPPG TMPEAAIEDL RKDLEL
Length:136
Mass (Da):14,748
Last modified:April 18, 2006 - v1
Checksum:i051735403943D06C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008230 Genomic DNA. Translation: BAE85025.1.
RefSeqiYP_519469.1. NC_007907.1.

Genome annotation databases

EnsemblBacteriaiBAE85025; BAE85025; DSY3236.
KEGGidsy:DSY3236.
PATRICi21675368. VBIDesHaf65307_3612.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008230 Genomic DNA. Translation: BAE85025.1.
RefSeqiYP_519469.1. NC_007907.1.

3D structure databases

SMRiQ24SG7. Positions 1-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi138119.DSY3236.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE85025; BAE85025; DSY3236.
KEGGidsy:DSY3236.
PATRICi21675368. VBIDesHaf65307_3612.

Phylogenomic databases

eggNOGiCOG2185.
HOGENOMiHOG000011065.
KOiK01846.
OMAiGHGEMDC.
OrthoDBiEOG6CP428.

Enzyme and pathway databases

UniPathwayiUPA00561; UER00617.
BioCyciDHAF138119:GHT5-3308-MONOMER.

Family and domain databases

Gene3Di3.40.50.280. 1 hit.
HAMAPiMF_00526. Me_Asp_mutase_S.
InterProiIPR006159. Acid_CoA_mut_C.
IPR006158. Cobalamin-bd.
IPR006394. GlmS.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR01501. MthylAspMutase. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the dehalorespiring bacterium Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides ethenogenes 195."
    Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., Inatomi K., Furukawa K., Inui M., Yukawa H.
    J. Bacteriol. 188:2262-2274(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Y51.

Entry informationi

Entry nameiGMSS_DESHY
AccessioniPrimary (citable) accession number: Q24SG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: April 18, 2006
Last modified: April 29, 2015
This is version 66 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.