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Q32IJ3

- GMSS_SHIDS

UniProt

Q32IJ3 - GMSS_SHIDS

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Protein

Glutamate mutase sigma subunit

Gene

glmS

Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Status
Reviewed - 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

BioCyciSDYS300267:GJEW-672-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
Ordered Locus Names:SDY_0676
OrganismiShigella dysenteriae serotype 1 (strain Sd197)
Taxonomic identifieri300267 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000002716: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 149149Glutamate mutase sigma subunitPRO_0000264143Add
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

STRINGi300267.SDY_0676.

Structurei

3D structure databases

ProteinModelPortaliQ32IJ3.
SMRiQ32IJ3. Positions 1-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 140138B12-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.
OrthoDBiEOG6CP428.

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.

Q32IJ3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKATLVIGV IGADCHAVGN KVLDRVFSNH DFRVINLGVM VSQDEYIDAA
60 70 80 90 100
IETGADAIVV SSIYGHGDID CLGMRERCIE RGLGDILLYV GGNLVVGKHD
110 120 130 140
FADVETKFKE MGFDRVFAPS HDLEDVCQLM AHDINQRHDV DTRILEEAI
Length:149
Mass (Da):16,430
Last modified:December 12, 2006 - v2
Checksum:iB785DAE49F27D9D0
GO

Sequence cautioni

The sequence ABB60864.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000034 Genomic DNA. Translation: ABB60864.1. Different initiation.
RefSeqiYP_402353.1. NC_007606.1.

Genome annotation databases

EnsemblBacteriaiABB60864; ABB60864; SDY_0676.
GeneIDi3799220.
KEGGisdy:SDY_0676.
PATRICi18690633. VBIShiDys99784_0789.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000034 Genomic DNA. Translation: ABB60864.1 . Different initiation.
RefSeqi YP_402353.1. NC_007606.1.

3D structure databases

ProteinModelPortali Q32IJ3.
SMRi Q32IJ3. Positions 1-119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300267.SDY_0676.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB60864 ; ABB60864 ; SDY_0676 .
GeneIDi 3799220.
KEGGi sdy:SDY_0676.
PATRICi 18690633. VBIShiDys99784_0789.

Phylogenomic databases

eggNOGi COG2185.
HOGENOMi HOG000011065.
KOi K01846.
OrthoDBi EOG6CP428.

Enzyme and pathway databases

UniPathwayi UPA00561 ; UER00617 .
BioCyci SDYS300267:GJEW-672-MONOMER.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sd197.

Entry informationi

Entry nameiGMSS_SHIDS
AccessioniPrimary (citable) accession number: Q32IJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: November 26, 2014
This is version 60 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

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