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P61191

- GMSS_TREDE

UniProt

P61191 - GMSS_TREDE

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Protein

Glutamate mutase sigma subunit

Gene

glmS

Organism
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
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 bindingi17 – 171Cobalt (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

BioCyciTDEN243275:GJ7G-1037-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:TDE_1023
OrganismiTreponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Taxonomic identifieri243275 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema
ProteomesiUP000008212: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139Glutamate mutase sigma subunitPRO_0000216448Add
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

STRINGi243275.TDE1023.

Structurei

3D structure databases

ProteinModelPortaliP61191.
SMRiP61191. Positions 4-131.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 139136B12-bindingUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 185Adenosylcobalamin bindingUniRule annotation
Regioni62 – 643Adenosylcobalamin bindingUniRule annotation
Regioni94 – 985Adenosylcobalamin bindingUniRule annotation

Sequence similaritiesi

Belongs to the methylaspartate mutase GlmS subunit family.UniRule annotation
Contains 1 B12-binding domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG2185.
KOiK01846.
OMAiLNGHAYE.
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.

P61191-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARKIKLVLG VIGSDCHAVG NKILDYSLTE AGFEVTNIGV LSPQEDFINA
60 70 80 90 100
ALETNADAIL VSSLYGQGEL DCKGLREKCD EAGLKGIKLF VGGNIVVGKQ
110 120 130
NFDEVHKRFT AMGFDHVYPP GTPVETTIKD LHADFPDHA
Length:139
Mass (Da):14,988
Last modified:May 10, 2004 - v1
Checksum:iD43FFA8217AA6F15
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017226 Genomic DNA. Translation: AAS11512.1.
RefSeqiNP_971631.1. NC_002967.9.

Genome annotation databases

EnsemblBacteriaiAAS11512; AAS11512; TDE_1023.
GeneIDi2741502.
KEGGitde:TDE1023.
PATRICi20524254. VBITreDen445_0985.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017226 Genomic DNA. Translation: AAS11512.1 .
RefSeqi NP_971631.1. NC_002967.9.

3D structure databases

ProteinModelPortali P61191.
SMRi P61191. Positions 4-131.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243275.TDE1023.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAS11512 ; AAS11512 ; TDE_1023 .
GeneIDi 2741502.
KEGGi tde:TDE1023.
PATRICi 20524254. VBITreDen445_0985.

Phylogenomic databases

eggNOGi COG2185.
KOi K01846.
OMAi LNGHAYE.
OrthoDBi EOG6CP428.

Enzyme and pathway databases

UniPathwayi UPA00561 ; UER00617 .
BioCyci TDEN243275:GJ7G-1037-MONOMER.

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 35405 / CIP 103919 / DSM 14222.

Entry informationi

Entry nameiGMSS_TREDE
AccessioniPrimary (citable) accession number: P61191
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: November 26, 2014
This is version 76 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