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Q05488 (MAMA_CLOTT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:mutS
OrganismClostridium tetanomorphum
Taxonomic identifier1553 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

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

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. E exists as a homodimer and S as a monomer.

Sequence similarities

Contains 1 B12-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 137137Methylaspartate mutase S chain HAMAP-Rule MF_00526
PRO_0000216445

Regions

Domain3 – 137135B12-binding

Sites

Metal binding161Cobalt (cobalamin axial ligand)

Secondary structure

1 .............................. 137
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05488 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: E71FE55BA8CE3DB3

FASTA13714,748
        10         20         30         40         50         60 
MEKKTIVLGV IGSDCHAVGN KILDHSFTNA GFNVVNIGVL SSQEDFINAA IETKADLICV 

        70         80         90        100        110        120 
SSLYGQGEID CKGLREKCDE AGLKGIKLFV GGNIVVGKQN WPDVEQRFKA MGFDRVYPPG 

       130 
TSPETTIADM KEVLGVE

« Hide

References

[1]"Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes."
Marsh E.N.G., Holloway D.E.
FEBS Lett. 310:167-170(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-33.
Strain: NCIMB 11547.
[2]"Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum."
Brecht M., Kellermann J., Plueckthun A.
FEBS Lett. 319:84-89(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-24.
Strain: ATCC 15920 / DSM 528 / H1.
[3]"How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum."
Tollinger M., Konrat R., Hilbert B.H., Marsh E.N.G., Kraeutler B.
Structure 6:1021-1033(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
Strain: ATCC 15920 / DSM 528 / H1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X70499 Genomic DNA. Translation: CAA49908.1.
X68570 Genomic DNA. Translation: CAA48567.1.
PIRS29502.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE1NMR-A1-137[»]
1FMFNMR-A1-137[»]
1ID8NMR-A1-137[»]
ProteinModelPortalQ05488.
SMRQ05488. Positions 1-137.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ05488.
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. Cbl-bd. 1 hit.
TIGRFAMsTIGR01501. MthylAspMutase. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ05488.

Entry information

Entry nameMAMA_CLOTT
AccessionPrimary (citable) accession number: Q05488
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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