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P11652 (MUTA_PROFR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 94. 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:
Methylmalonyl-CoA mutase small subunit
EC=5.4.99.2
Alternative name(s):
MCB-beta
Gene names
Name:mutA
OrganismPropionibacterium freudenreichii subsp. shermanii
Taxonomic identifier1752 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.

Catalytic activity

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

Cofactor

Adenosylcobalamin.

Pathway

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

Subunit structure

Heterodimer of an alpha and a beta chain.

Sequence similarities

Belongs to the methylmalonyl-CoA mutase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mutBP116534EBI-1027328,EBI-1027336

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 638637Methylmalonyl-CoA mutase small subunit
PRO_0000194268

Secondary structure

1 ..................................................................................................... 638
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11652 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F44C708AA8D47075

FASTA63869,464
        10         20         30         40         50         60 
MSSTDQGTNP ADTDDLTPTT LSLAGDFPKA TEEQWEREVE KVLNRGRPPE KQLTFAECLK 

        70         80         90        100        110        120 
RLTVHTVDGI DIVPMYRPKD APKKLGYPGV APFTRGTTVR NGDMDAWDVR ALHEDPDEKF 

       130        140        150        160        170        180 
TRKAILEGLE RGVTSLLLRV DPDAIAPEHL DEVLSDVLLE MTKVEVFSRY DQGAAAEALV 

       190        200        210        220        230        240 
SVYERSDKPA KDLALNLGLD PIAFAALQGT EPDLTVLGDW VRRLAKFSPD SRAVTIDANI 

       250        260        270        280        290        300 
YHNAGAGDVA ELAWALATGA EYVRALVEQG FTATEAFDTI NFRVTATHDQ FLTIARLRAL 

       310        320        330        340        350        360 
REAWARIGEV FGVDEDKRGA RQNAITSWRD VTREDPYVNI LRGSIATFSA SVGGAESITT 

       370        380        390        400        410        420 
LPFTQALGLP EDDFPLRIAR NTGIVLAEEV NIGRVNDPAG GSYYVESLTR SLADAAWKEF 

       430        440        450        460        470        480 
QEVEKLGGMS KAVMTEHVTK VLDACNAERA KRLANRKQPI TAVSEFPMIG ARSIETKPFP 

       490        500        510        520        530        540 
AAPARKGLAW HRDSEVFEQL MDRSTSVSER PKVFLACLGT RRDFGGREGF SSPVWHIAGI 

       550        560        570        580        590        600 
DTPQVEGGTT AEIVEAFKKS GAQVADLCSS AKVYAQQGLE VAKALKAAGA KALYLSGAFK 

       610        620        630 
EFGDDAAEAE KLIDGRLFMG MDVVDTLSST LDILGVAK

« Hide

References

[1]"Cloning and structural characterization of the genes coding for adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii."
Marsh E.N., McKie N., Davis N.K., Leadlay P.F.
Biochem. J. 260:345-352(1989) [PubMed: 2569861] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 4-9; 96-100; 302-306; 473-478 AND 523-527.
Strain: NCIB 9885.
[2]"Methylmalonyl-CoA mutase from Propionibacterium shermanii. Evidence for the presence of two masked cysteine residues."
Marsh E.N., Leadlay P.F.
Biochem. J. 260:339-343(1989) [PubMed: 2569860] [Abstract]
Cited for: PROTEIN SEQUENCE OF 515-518.
Strain: NCIB 9885.
[3]"How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2-A resolution."
Mancia F., Keep N.H., Nakagawa A., Leadlay P.F., McSweeney S., Rasmussen B., Bosecke P., Diat O., Evans P.R.
Structure 4:339-350(1996) [PubMed: 8805541] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: NCIB 9885.
[4]"Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism."
Mancia F., Evans P.R.
Structure 6:711-720(1998) [PubMed: 9655823] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Strain: NCIB 9885.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X14965 Genomic DNA. Translation: CAA33089.1.
PIRS04640.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E1CX-ray2.62B/D2-637[»]
1REQX-ray2.00B/D2-638[»]
2REQX-ray2.50B/D2-638[»]
3REQX-ray2.70B2-638[»]
4REQX-ray2.20B/D2-638[»]
5REQX-ray2.20B/D2-637[»]
6REQX-ray2.20B/D2-637[»]
7REQX-ray2.20B/D2-637[»]
ProteinModelPortalP11652.
SMRP11652. Positions 16-638.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6149N.
IntActP11652. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13076.

Family and domain databases

InterProIPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR024067. Me-malonyl-CoA_mutase_sm_su_N.
IPR006099. MeMalonylCoA_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.
G3DSA:1.10.196.20. G3DSA:1.10.196.20. 1 hit.
PfamPF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
SUPFAMSSF52242. Cbl-bd. 1 hit.
SSF51703. Cbl-dep_enz_cat. 1 hit.
TIGRFAMsTIGR00642. MmCoA_mut_beta. 1 hit.
PROSITEPS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMUTA_PROFR
AccessionPrimary (citable) accession number: P11652
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 94 of the entry and version 3 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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