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Reviewed, UniProtKB/Swiss-Prot Q05488 (MAMA_CLOTT)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Cofactor

5'-deoxy-5'-adenosyl-adeninylcobamide (pseudo-coenzyme B12). HAMAP MF_00526

Pathway

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

Subunit structure

Heterotetramer of 2 E subunits and 2 S subunits. E exists as a homodimer and S as a monomer. HAMAP MF_00526

Sequence similarities

Contains 1 B12-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 137137Methylaspartate mutase S chain HAMAP MF_00526
PRO_0000216445

Regions

Domain3 – 137135B12-binding

Sites

Metal binding161Cobalt (cobalamin axial ligand) HAMAP MF_00526

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05488-1 [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: 1397267] [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: 8454064] [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: 9739092] [Abstract]
Cited for: STRUCTURE BY NMR.
Strain: ATCC 15920 / DSM 528 / H1.
+Additional computationally mapped references.

Cross-references

Sequence databases

X70499 Genomic DNA. Translation: CAA49908.1.
X68570 Genomic DNA. Translation: CAA48567.1.
PIRS29502.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BE1NMR-A1-137[»]
1FMFNMR-A1-137[»]
1ID8NMR-A1-137[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.4.99.1. 2080.

Family and domain databases

HAMAPMF_00526.
[Tree]
InterProIPR006158. Cobalamin-bd.
IPR006394. Met_Asp_mutase.
[Graphical view]
Gene3DG3DSA:3.40.50.280. B12_bd. 1 hit.
PfamPF02310. B12-binding. 1 hit.
[Graphical view]
TIGRFAMsTIGR01501. MthylAspMutase. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents