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Protein
Submitted name:

Methylmalonyl CoA epimerase

Gene
N/A
Organism
Propionibacterium freudenreichii subsp. shermanii
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei48 – 481Sulfate 1Combined sources
Binding sitei65 – 651Sulfate 1Combined sources
Binding sitei65 – 651Sulfate 2Combined sources
Binding sitei122 – 1221Sulfate 1Combined sources
Binding sitei122 – 1221Sulfate 2Combined sources
Binding sitei141 – 1411Sulfate 1Combined sources
Binding sitei141 – 1411Sulfate 2Combined sources

GO - Molecular functioni

  1. methylmalonyl-CoA epimerase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

IsomeraseImported

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13075.

Names & Taxonomyi

Protein namesi
Submitted name:
Methylmalonyl CoA epimeraseImported (EC:5.1.99.1Imported)
Submitted name:
Methylmalonyl-CoA epimeraseImported (EC:5.1.99.1Imported)
OrganismiPropionibacterium freudenreichii subsp. shermaniiImported
Taxonomic identifieri1752 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JC4X-ray2.00A/B/C/D1-148[»]
1JC5X-ray2.20A/B/C/D/E/F1-148[»]
ProteinModelPortaliQ8VQN0.
SMRiQ8VQN0. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8VQN0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 603Sulfate 3 bindingCombined sources
Regioni58 – 603Sulfate 4 bindingCombined sources
Regioni116 – 1172Sulfate 5 bindingCombined sources

Family and domain databases

Gene3Di3.10.180.10. 1 hit.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR017515. MeMalonyl-CoA_epimerase.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR03081. metmalonyl_epim. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8VQN0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNEDLFICI DHVAYACPDA DEASKYYQET FGWHELHREE NPEQGVVEIM
60 70 80 90 100
MAPAAKLTEH MTQVQVMAPL NDESTVAKWL AKHNGRAGLH HMAWRVDDID
110 120 130 140
AVSATLRERG VQLLYDEPKL GTGGNRINFM HPKSGKGVLI ELTQYPKN
Length:148
Mass (Da):16,717
Last modified:March 1, 2002 - v1
Checksum:i258F88915E03F598
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046899 Genomic DNA. Translation: AAL02261.1.
AF454511 Genomic DNA. Translation: AAL57846.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046899 Genomic DNA. Translation: AAL02261.1.
AF454511 Genomic DNA. Translation: AAL57846.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JC4X-ray2.00A/B/C/D1-148[»]
1JC5X-ray2.20A/B/C/D/E/F1-148[»]
ProteinModelPortaliQ8VQN0.
SMRiQ8VQN0. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13075.

Miscellaneous databases

EvolutionaryTraceiQ8VQN0.

Family and domain databases

Gene3Di3.10.180.10. 1 hit.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR017515. MeMalonyl-CoA_epimerase.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR03081. metmalonyl_epim. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The structural genes for methylmalonyl CoA metabolism in Propionibacterium shermanii."
    Davis N.K.
    Thesis (1985), University of Cambridge
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: NCIB 9885Imported.
  2. "Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: a novel enzymatic function on an ancient metal binding scaffold."
    McCarthy A.A., Baker H.M., Shewry S.C., Patchett M.L., Baker E.N.
    Structure 9:637-646(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: NCIB 9885Imported.
  3. "Metabolic engineering of a methylmalonyl-CoA mutase-epimerase pathway for complex polyketide biosynthesis in Escherichia coli."
    Dayem L.C., Santi D.V., Pfeifer B.A., Khosla C., Kealey J.T.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. Davis N.K., Leadlay P.F., Patchett M.L.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: NCIB 9885Imported.

Entry informationi

Entry nameiQ8VQN0_PROFR
AccessioniPrimary (citable) accession number: Q8VQN0
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2002
Last sequence update: March 1, 2002
Last modified: April 1, 2015
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.