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Reviewed, UniProtKB/Swiss-Prot Q05064 (MUTA_STRCM)

Last modified June 16, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Methylmalonyl-CoA mutase small subunit
    EC=5.4.99.2
Alternative name(s):
    MCM-beta
Gene names
Name: mutA
OrganismStreptomyces cinnamonensis
Taxonomic identifier1900 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length616 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. This conversion most likely represents an important source of building blocks for polyketide antibiotic biosynthesis. It is unable to catalyze the conversion of isobutyryl-CoA into N-butyryl-CoA.

Catalytic activity

(R)-methylmalonyl-CoA = succinyl-CoA.

Cofactor

Adenosylcobalamin.

Pathway

Metabolic intermediate metabolism; propionyl-CoA degradation; succinyl-CoA from propionyl-CoA: step 3/3.

Subunit structure

Heterodimer of an alpha and a beta chain.

Sequence similarities

Belongs to the methylmalonyl-CoA mutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 616616Methylmalonyl-CoA mutase small subunit
PRO_0000194269

Sequences

Sequence LengthMass (Da)Tools
Q05064-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 09CA24006E169AE6

FASTA61665,041
        10         20         30         40         50         60 
MTVLPDDGLS LAAEFPDATH EQWHRLVEGV VRKSGKDVSG TAAEEALSTT LEDGLTTRPL 

        70         80         90        100        110        120 
YTARDAAPDA GFPGFAPFVR GSVPEGNTPG GWDVRQRYAS ADPARTNEAV LTDLENGVTS 

       130        140        150        160        170        180 
LWLTLGSAGL PVTGLERALD GVYLDLVPVA LDAGSEAATA ARELLRLYEA AGVADDAVRG 

       190        200        210        220        230        240 
TLGADPLGHE ARTGEKSTSF AAVAELARLC GERYPGLRAL TVDALPYHEA GASAAQELGA 

       250        260        270        280        290        300 
SLATGVEYLR ALHDKGLGVE KAFAQLEFRF AATADQFLTI AKLRAARRLW ARVAEVSGVP 

       310        320        330        340        350        360 
AAGAQRQHAV TSPVMMTRRD PWVNMLRTTV ACLGAGVGGA DAVTVLPFDH ELGLPDAFAR 

       370        380        390        400        410        420 
RIARNTSTIL LEESHLARVI DPAGGSWYVE RLTDELAHAA WDFFKEIERA DGQVAALRSG 

       430        440        450        460        470        480 
LVGDRIAATW AERRKKLARR REPITGVSEF PLLTERPVER EPAPAAPPGG LPRVRRDEAY 

       490        500        510        520        530        540 
EELRGRSDAH LEATGARPKV FIAALGPAAA HTARATFAAN LFMAGGVEPV HDPVSVDAET 

       550        560        570        580        590        600 
AAEAFAASGA TVACLCSSDV LYAEQAEAVA RALKSAGALR VFLAGRGEFA DIDEYVFAGC 

       610 
DAVAVLTSTL DRMGVA 

« Hide

References

[1]"Cloning, sequencing, and expression of the gene encoding methylmalonyl-coenzyme A mutase from Streptomyces cinnamonensis."
Birch A., Leiser A., Robinson J.A.
J. Bacteriol. 175:3511-3519(1993) [PubMed: 8099072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A3823.5.

Cross-references

Sequence databases

L10064 Unassigned DNA. Translation: AAA03040.1.
PIRA40595.

3D structure databases

HSSPHSSP built from PDB template 2REQ based on UniProtKB P11652.
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.4.99.2. 1647.

Family and domain databases

InterProIPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR006099. MMCoA_mutase_a/b_cat.
IPR004608. MMCoA_mutase_b.
[Graphical view]
Gene3DG3DSA:3.40.50.280. B12_bd. 1 hit.
G3DSA:3.20.20.240. Cobalamin-dep_enz_cat. 1 hit.
PfamPF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00642. mmCoA_mut_beta. 1 hit.
PROSITEPS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMUTA_STRCM
AccessionPrimary (citable) accession number: Q05064
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 51 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

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