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Reviewed, UniProtKB/Swiss-Prot Q05065 (MUTB_STRCM)

Last modified June 16, 2009. Version 57. 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 large subunit
    EC=5.4.99.2
Alternative name(s):
    MCM-alpha
Gene names
Name: mutB
OrganismStreptomyces cinnamonensis
Taxonomic identifier1900 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length733 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.

Contains 1 B12-binding domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 733733Methylmalonyl-CoA mutase large subunit
PRO_0000194275

Regions

Domain600 – 732133B12-binding
Region571 – 61040Methylmalonyl-CoA-binding site By similarity

Sites

Metal binding6131Cobalt (cobalamin axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q05065-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: F02EEB54A154FA59

FASTA73379,455
        10         20         30         40         50         60 
MRIPEFDDIE LGAGGGPSGS AEQWRAAVKE SVGKSESDLL WETPEGIAVK PLYTGADVEG 

        70         80         90        100        110        120 
LDFLETYPGV APYLRGPYPT MYVNQPWTIR QYAGFSTAEE SNAFYRRNLA AGQKGLSVAF 

       130        140        150        160        170        180 
DLPTHRGYDS DHPRVTGDVG MAGVAIDSIY DMRQLFDGIP LDKMTVSMTM NGAVLPVLAL 

       190        200        210        220        230        240 
YIVAAEEQGV PPEKLAGTIQ NDILKEFMVR NTYIYPPKPS MRIISDIFAY TSQKMPRYNS 

       250        260        270        280        290        300 
ISISGYHIQE AGATADLELA YTLADGVEYL RAGQEAGLDV DAFAPRLSFF WAIGMNFFME 

       310        320        330        340        350        360 
VAKLRAARLL WAKLVKQFDP KNAKSLSLRT HSQTSGWSLT AQDVFNNVTR TCVEAMAATQ 

       370        380        390        400        410        420 
GHTQSLHTNA LDEALALPTD FSARIARNTQ LLIQQESGTT RTIDPWGGSA YVEKLTYDLA 

       430        440        450        460        470        480 
RRAWQHIEEV EAAGGMAQAI DAGIPKLRVE EAAARTQARI DSGRQPVIGV NKYRVDTDEQ 

       490        500        510        520        530        540 
IDVLKVDNSS VRAQQIEKLR RLREERDDAA CQDALRALTA AAERGPGQGL EGNLLALAVD 

       550        560        570        580        590        600 
AARAKATVGE ISDALESVYG RHAGQIRTIS GVYRTEAGQS PSVERTRALV DAFDEAEGRR 

       610        620        630        640        650        660 
PRILVAKMGQ DGHDRGQKVI ASAFADLGFD VDVGPLFQTP AEVARQAVEA DVHIVGVSSL 

       670        680        690        700        710        720 
AAGHLTLVPA LREELAAEGR DDIMIVVGGV IPPQDVEALH EAGATAVFPP GTVIPDAAHD 

       730 
LVKRLAADLG HEL 

« 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: AAA03041.1.
PIRB40595.

3D structure databases

HSSPHSSP built from PDB template 1REQ based on UniProtKB P11653.
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.4.99.2. 1647.

Family and domain databases

InterProIPR006159. Acid_CoA_mut_C.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR006099. MMCoA_mutase_a/b_cat.
IPR006098. MMCoA_mutase_a_cat.
[Graphical view]
Gene3DG3DSA:3.40.50.280. B12_bd. 1 hit.
G3DSA:3.20.20.240. Cobalamin-dep_enz_cat. 1 hit.
PfamPF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMUTB_STRCM
AccessionPrimary (citable) accession number: Q05065
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 57 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