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Q32IJ3

- GMSS_SHIDS

UniProt

Q32IJ3 - GMSS_SHIDS

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Protein
Glutamate mutase sigma subunit
Gene
glmS, SDY_0676
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) By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Adenosylcobalamin By similarity.UniRule annotation

Pathwayi

Sites

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

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 subunit (EC:5.4.99.1)
Alternative name(s):
Glutamate mutase S chain
Glutamate mutase small subunit
Methylaspartate mutase
Gene namesi
Name:glmS
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 subunitUniRule annotation
PRO_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 By similarity.

Protein-protein interaction databases

STRINGi300267.SDY_0676.

Structurei

3D structure databases

ProteinModelPortaliQ32IJ3.
SMRiQ32IJ3. Positions 1-119.

Family & Domainsi

Domains and Repeats

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

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

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MKKATLVIGV IGADCHAVGN KVLDRVFSNH DFRVINLGVM VSQDEYIDAA    50
IETGADAIVV SSIYGHGDID CLGMRERCIE RGLGDILLYV GGNLVVGKHD 100
FADVETKFKE MGFDRVFAPS HDLEDVCQLM AHDINQRHDV DTRILEEAI 149
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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: July 9, 2014
This is version 58 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

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