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Q3AFA7 (GMSS_CARHZ) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate mutase sigma subunit

EC=5.4.99.1
Alternative name(s):
Glutamate mutase S chain
Glutamate mutase small subunit
Methylaspartate mutase
Gene names
Name:glmS
Synonyms:mamA
Ordered Locus Names:CHY_0307
OrganismCarboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [Complete proteome] [HAMAP]
Taxonomic identifier246194 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCarboxydothermus

Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate) By similarity. HAMAP-Rule MF_00526

Catalytic activity

L-threo-3-methylaspartate = L-glutamate. HAMAP-Rule MF_00526

Cofactor

Adenosylcobalamin By similarity. HAMAP-Rule MF_00526

Pathway

Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 1/4. HAMAP-Rule MF_00526

Subunit structure

Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer By similarity.

Sequence similarities

Belongs to the methylaspartate mutase GlmS subunit family.

Contains 1 B12-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 137137Glutamate mutase sigma subunit HAMAP-Rule MF_00526
PRO_0000264141

Regions

Domain3 – 137135B12-binding
Region13 – 175Adenosylcobalamin binding By similarity
Region61 – 633Adenosylcobalamin binding By similarity
Region93 – 975Adenosylcobalamin binding By similarity

Sites

Metal binding161Cobalt (cobalamin axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3AFA7 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 1E07CACA4631E49D

FASTA13714,868
        10         20         30         40         50         60 
MKEVNLVLGV IGADVHAIGN KILEYALTNA GFKVHNLGVM VSQEEFVKAA LETDAKAVLV 

        70         80         90        100        110        120 
SSLYGHGEID CRGLKEKFIE AGLDDVLLYV GGNLVVGKQD FSEVERKFKA MGFDRVFPPG 

       130 
TMPEEAIKAL KEDLGLM 

« Hide

References

[1]"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901."
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.
PLoS Genet. 1:563-574(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Z-2901 / DSM 6008.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000141 Genomic DNA. Translation: ABB15477.1.
RefSeqYP_359177.1. NC_007503.1.

3D structure databases

ProteinModelPortalQ3AFA7.
SMRQ3AFA7. Positions 1-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246194.CHY_0307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB15477; ABB15477; CHY_0307.
GeneID3727582.
KEGGchy:CHY_0307.
PATRIC21273785. VBICarHyd26463_0291.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2185.
HOGENOMHOG000011065.
KOK01846.
OMAMGFNRVF.
OrthoDBEOG6CP428.

Enzyme and pathway databases

BioCycCHYD246194:GJCN-308-MONOMER.
UniPathwayUPA00561; UER00617.

Family and domain databases

Gene3D3.40.50.280. 1 hit.
HAMAPMF_00526. Me_Asp_mutase_S.
InterProIPR006159. Acid_CoA_mut_C.
IPR006158. Cobalamin-bd.
IPR006394. Me_Asp_mutase.
[Graphical view]
PfamPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMSSF52242. SSF52242. 1 hit.
TIGRFAMsTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR01501. MthylAspMutase. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGMSS_CARHZ
AccessionPrimary (citable) accession number: Q3AFA7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 22, 2005
Last modified: July 9, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways