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Q3AFA7

- GMSS_CARHZ

UniProt

Q3AFA7 - GMSS_CARHZ

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Protein
Glutamate mutase sigma subunit
Gene
glmS, mamA, CHY_0307
Organism
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
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

BioCyciCHYD246194:GJCN-308-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:mamA
Ordered Locus Names:CHY_0307
OrganismiCarboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Taxonomic identifieri246194 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCarboxydothermus
ProteomesiUP000002706: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Glutamate mutase sigma subunitUniRule annotation
PRO_0000264141Add
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

STRINGi246194.CHY_0307.

Structurei

3D structure databases

ProteinModelPortaliQ3AFA7.
SMRiQ3AFA7. Positions 1-136.

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.
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.

Q3AFA7-1 [UniParc]FASTAAdd to Basket

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MKEVNLVLGV IGADVHAIGN KILEYALTNA GFKVHNLGVM VSQEEFVKAA    50
LETDAKAVLV SSLYGHGEID CRGLKEKFIE AGLDDVLLYV GGNLVVGKQD 100
FSEVERKFKA MGFDRVFPPG TMPEEAIKAL KEDLGLM 137
Length:137
Mass (Da):14,868
Last modified:November 22, 2005 - v1
Checksum:i1E07CACA4631E49D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000141 Genomic DNA. Translation: ABB15477.1.
RefSeqiWP_011343253.1. NC_007503.1.
YP_359177.1. NC_007503.1.

Genome annotation databases

EnsemblBacteriaiABB15477; ABB15477; CHY_0307.
GeneIDi3727582.
KEGGichy:CHY_0307.
PATRICi21273785. VBICarHyd26463_0291.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000141 Genomic DNA. Translation: ABB15477.1 .
RefSeqi WP_011343253.1. NC_007503.1.
YP_359177.1. NC_007503.1.

3D structure databases

ProteinModelPortali Q3AFA7.
SMRi Q3AFA7. Positions 1-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 246194.CHY_0307.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB15477 ; ABB15477 ; CHY_0307 .
GeneIDi 3727582.
KEGGi chy:CHY_0307.
PATRICi 21273785. VBICarHyd26463_0291.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00561 ; UER00617 .
BioCyci CHYD246194:GJCN-308-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: Z-2901 / DSM 6008.

Entry informationi

Entry nameiGMSS_CARHZ
AccessioniPrimary (citable) accession number: Q3AFA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 22, 2005
Last modified: September 3, 2014
This is version 65 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

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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