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P58620 (MAMA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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:
Methylaspartate mutase S chain

EC=5.4.99.1
Alternative name(s):
Glutamate mutase subunit sigma
Gene names
Name:mamA
Ordered Locus Names:Z0895, ECs0764
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

5'-deoxy-5'-adenosyl-adeninylcobamide (pseudo-coenzyme B12) By similarity.

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 of 2 E subunits and 2 S subunits By similarity.

Sequence similarities

Contains 1 B12-binding domain.

Sequence caution

The sequence AAG55064.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 149149Methylaspartate mutase S chain HAMAP-Rule MF_00526
PRO_0000216446

Regions

Domain3 – 140138B12-binding

Sites

Metal binding161Cobalt (cobalamin axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P58620 [UniParc].

Last modified January 23, 2002. Version 1.
Checksum: B785DAE49F27D9D0

FASTA14916,430
        10         20         30         40         50         60 
MKKATLVIGV IGADCHAVGN KVLDRVFSNH DFRVINLGVM VSQDEYIDAA IETGADAIVV 

        70         80         90        100        110        120 
SSIYGHGDID CLGMRERCIE RGLGDILLYV GGNLVVGKHD FADVETKFKE MGFDRVFAPS 

       130        140 
HDLEDVCQLM AHDINQRHDV DTRILEEAI 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG55064.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB34187.1.
PIRD85575.
D90724.
RefSeqNP_286456.1. NC_002655.2.
NP_308791.1. NC_002695.1.

3D structure databases

ProteinModelPortalP58620.
SMRP58620. Positions 1-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z0895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG55064; AAG55064; Z0895.
BAB34187; BAB34187; BAB34187.
GeneID917503.
957856.
KEGGece:Z0895.
ecs:ECs0764.
PATRIC18350552. VBIEscCol44059_0787.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2185.
HOGENOMHOG000011065.
KOK01846.
OMAHAVGNKI.
OrthoDBEOG6CP428.
ProtClustDBPRK02261.

Enzyme and pathway databases

BioCycECOL386585:GJFA-759-MONOMER.
UniPathwayUPA00561; UER00617.

Family and domain databases

Gene3D3.40.50.280. 1 hit.
HAMAPMF_00526. MthylAspMutase_S.
InterProIPR006158. Cobalamin-bd.
IPR006394. Me_Asp_mutase.
[Graphical view]
PfamPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMSSF52242. SSF52242. 1 hit.
TIGRFAMsTIGR01501. MthylAspMutase. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMAMA_ECO57
AccessionPrimary (citable) accession number: P58620
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: February 19, 2014
This is version 73 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