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Q890S0

- GMSS_CLOTE

UniProt

Q890S0 - GMSS_CLOTE

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Protein
Glutamate mutase sigma subunit
Gene
glmS, mutS, CTC_02568
Organism
Clostridium tetani (strain Massachusetts / E88)
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

BioCyciCTET212717:GJAM-2372-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
Synonyms:mutS
Ordered Locus Names:CTC_02568
OrganismiClostridium tetani (strain Massachusetts / E88)
Taxonomic identifieri212717 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001412: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Glutamate mutase sigma subunitUniRule annotation
PRO_0000216444Add
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

STRINGi212717.CTC02568.

Structurei

3D structure databases

ProteinModelPortaliQ890S0.
SMRiQ890S0. Positions 1-137.

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.

Phylogenomic databases

eggNOGiCOG2185.
KOiK01846.
OMAiTSQEEFA.
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.

Q890S0-1 [UniParc]FASTAAdd to Basket

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MEKKTIVLGV IGSDCHAVGN KILDHSFTAA GFNVVNIGVL SPQEDFINAA    50
IETKADAILV SSLYGQGEID CKGLRQKCDE AGLEGILLYV GGNIVVGKQH 100
WPDVEKRFKD MGYDRVYAPG TPPEVGIADL KEDLNIK 137
Length:137
Mass (Da):14,773
Last modified:May 30, 2003 - v1
Checksum:i9BDE133E7A8D0035
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015927 Genomic DNA. Translation: AAO37025.1.
RefSeqiNP_783088.1. NC_004557.1.

Genome annotation databases

EnsemblBacteriaiAAO37025; AAO37025; CTC_02568.
GeneIDi1060139.
KEGGictc:CTC02568.
PATRICi19513251. VBICloTet101274_2656.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated