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Q8RHY7

- GMSS_FUSNN

UniProt

Q8RHY7 - GMSS_FUSNN

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Protein
Glutamate mutase sigma subunit
Gene
glmS, FN1853
Organism
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
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
Complete GO annotation...

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

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:FN1853
OrganismiFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Taxonomic identifieri190304 [NCBI]
Taxonomic lineageiBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium
ProteomesiUP000002521: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 136136Glutamate mutase sigma subunitUniRule annotation
PRO_0000216447Add
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

STRINGi190304.FN1853.

Structurei

3D structure databases

ProteinModelPortaliQ8RHY7.
SMRiQ8RHY7. Positions 1-136.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Contains 1 B12-binding domain.

Phylogenomic databases

eggNOGiCOG2185.
HOGENOMiHOG000011065.
KOiK01846.
OMAiMGFNRVF.
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. Me_Asp_mutase.
[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.

Q8RHY7-1 [UniParc]FASTAAdd to Basket

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MAKKKIVIGV IGSDCHTVGN KIIHNKLEES GFDVVNIGAL SPQIDFINAA    50
LETNSDAIIV SSIYGYGELD CQGIREKCNE YGLKDILLYI GGNIGSSNEK 100
WENTEKRFKE MGFDRIYKPG TPIEETIIDL KKDFKI 136
Length:136
Mass (Da):15,144
Last modified:June 1, 2002 - v1
Checksum:i934DB52D9D4B382C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009951 Genomic DNA. Translation: AAL93952.1.
RefSeqiNP_602653.1. NC_003454.1.

Genome annotation databases

EnsemblBacteriaiAAL93952; AAL93952; FN1853.
GeneIDi992530.
KEGGifnu:FN1853.
PATRICi21949229. VBIFusNuc122357_0329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009951 Genomic DNA. Translation: AAL93952.1 .
RefSeqi NP_602653.1. NC_003454.1.

3D structure databases

ProteinModelPortali Q8RHY7.
SMRi Q8RHY7. Positions 1-136.
ModBasei Search...

Protein-protein interaction databases

STRINGi 190304.FN1853.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL93952 ; AAL93952 ; FN1853 .
GeneIDi 992530.
KEGGi fnu:FN1853.
PATRICi 21949229. VBIFusNuc122357_0329.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00561 ; UER00617 .

Family and domain databases

Gene3Di 3.40.50.280. 1 hit.
HAMAPi MF_00526. Me_Asp_mutase_S.
InterProi IPR006159. Acid_CoA_mut_C.
IPR006158. Cobalamin-bd.
IPR006394. Me_Asp_mutase.
[Graphical view ]
Pfami PF02310. B12-binding. 1 hit.
[Graphical view ]
SUPFAMi SSF52242. SSF52242. 1 hit.
TIGRFAMsi TIGR00640. acid_CoA_mut_C. 1 hit.
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: ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131.

Entry informationi

Entry nameiGMSS_FUSNN
AccessioniPrimary (citable) accession number: Q8RHY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 79 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

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