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P27253 (SCPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylmalonyl-CoA mutase

Short name=MCM
EC=5.4.99.2
Gene names
Name:scpA
Synonyms:sbm, yliK
Ordered Locus Names:b2917, JW2884
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length714 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the interconversion of succinyl-CoA and methylmalonyl-CoA. Could be part of a pathway that converts succinate to propionate. Ref.4 Ref.5

Catalytic activity

(R)-methylmalonyl-CoA = succinyl-CoA. Ref.4 Ref.5

Cofactor

Adenosylcobalamin. Ref.4 Ref.5

Subunit structure

Homodimer. Interacts with ArgK. Ref.6

Sequence similarities

Belongs to the methylmalonyl-CoA mutase family.

Contains 1 B12-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 714714Methylmalonyl-CoA mutase
PRO_0000194277

Regions

Domain584 – 714131B12-binding

Sites

Metal binding5971Cobalt (cobalamin axial ligand) By similarity

Experimental info

Sequence conflict3561A → V in CAA47311. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P27253 [UniParc].

Last modified August 29, 2003. Version 2.
Checksum: 65222F5EB2F4633A

FASTA71477,871
        10         20         30         40         50         60 
MSNVQEWQQL ANKELSRREK TVDSLVHQTA EGIAIKPLYT EADLDNLEVT GTLPGLPPYV 

        70         80         90        100        110        120 
RGPRATMYTA QPWTIRQYAG FSTAKESNAF YRRNLAAGQK GLSVAFDLAT HRGYDSDNPR 

       130        140        150        160        170        180 
VAGDVGKAGV AIDTVEDMKV LFDQIPLDKM SVSMTMNGAV LPVLAFYIVA AEEQGVTPDK 

       190        200        210        220        230        240 
LTGTIQNDIL KEYLCRNTYI YPPKPSMRII ADIIAWCSGN MPRFNTISIS GYHMGEAGAN 

       250        260        270        280        290        300 
CVQQVAFTLA DGIEYIKAAI SAGLKIDDFA PRLSFFFGIG MDLFMNVAML RAARYLWSEA 

       310        320        330        340        350        360 
VSGFGAQDPK SLALRTHCQT SGWSLTEQDP YNNVIRTTIE ALAATLGGTQ SLHTNAFDEA 

       370        380        390        400        410        420 
LGLPTDFSAR IARNTQIIIQ EESELCRTVD PLAGSYYIES LTDQIVKQAR AIIQQIDEAG 

       430        440        450        460        470        480 
GMAKAIEAGL PKRMIEEASA REQSLIDQGK RVIVGVNKYK LDHEDETDVL EIDNVMVRNE 

       490        500        510        520        530        540 
QIASLERIRA TRDDAAVTAA LNALTHAAQH NENLLAAAVN AARVRATLGE ISDALEVAFD 

       550        560        570        580        590        600 
RYLVPSQCVT GVIAQSYHQS EKSASEFDAI VAQTEQFLAD NGRRPRILIA KMGQDGHDRG 

       610        620        630        640        650        660 
AKVIASAYSD LGFDVDLSPM FSTPEEIARL AVENDVHVVG ASSLAAGHKT LIPELVEALK 

       670        680        690        700        710 
KWGREDICVV AGGVIPPQDY AFLQERGVAA IYGPGTPMLD SVRDVLNLIS QHHD 

« Hide

References

« Hide 'large scale' references
[1]"Physical map location of the new Escherichia coli gene sbm."
Roy I., Leadlay P.F.
J. Bacteriol. 174:5763-5764(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli."
Haller T., Buckel T., Retey J., Gerlt J.A.
Biochemistry 39:4622-4629(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
Strain: K12 / MG1655 / ATCC 47076.
[5]"Metabolic engineering of a methylmalonyl-CoA mutase-epimerase pathway for complex polyketide biosynthesis in Escherichia coli."
Dayem L.C., Carney J.R., Santi D.V., Pfeifer B.A., Khosla C., Kealey J.T.
Biochemistry 41:5193-5201(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
[6]"Sleeping beauty mutase (sbm) is expressed and interacts with ygfd in Escherichia coli."
Froese D.S., Dobson C.M., White A.P., Wu X., Padovani D., Banerjee R., Haller T., Gerlt J.A., Surette M.G., Gravel R.A.
Microbiol. Res. 164:1-8(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH ARGK.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66836 Genomic DNA. Translation: CAA47311.1.
U28377 Genomic DNA. Translation: AAA69084.1.
U00096 Genomic DNA. Translation: AAC75954.1.
AP009048 Genomic DNA. Translation: BAE76981.1.
PIRD65076.
RefSeqNP_417392.1. NC_000913.3.
YP_491117.1. NC_007779.1.

3D structure databases

ProteinModelPortalP27253.
SMRP27253. Positions 28-701.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP27253. 6 interactions.
STRING511145.b2917.

Proteomic databases

PaxDbP27253.
PRIDEP27253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75954; AAC75954; b2917.
BAE76981; BAE76981; BAE76981.
GeneID12933336.
945576.
KEGGecj:Y75_p2848.
eco:b2917.
PATRIC32121248. VBIEscCol129921_3012.

Organism-specific databases

EchoBASEEB1414.
EcoGeneEG11444. scpA.

Phylogenomic databases

eggNOGCOG2185.
HOGENOMHOG000003917.
KOK01847.
OMAAQDVYNN.
OrthoDBEOG6423BW.
PhylomeDBP27253.
ProtClustDBPRK09426.

Enzyme and pathway databases

BioCycEcoCyc:METHYLMALONYL-COA-MUT-MONOMER.
ECOL316407:JW2884-MONOMER.
MetaCyc:METHYLMALONYL-COA-MUT-MONOMER.

Gene expression databases

GenevestigatorP27253.

Family and domain databases

Gene3D3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProIPR006159. Acid_CoA_mut_C.
IPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR006099. MeMalonylCoA_mutase_a/b_cat.
IPR006098. MMCoA_mutase_a_cat.
[Graphical view]
PfamPF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
SUPFAMSSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
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...

Other

PROP27253.

Entry information

Entry nameSCPA_ECOLI
AccessionPrimary (citable) accession number: P27253
Secondary accession number(s): Q2M9S5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 29, 2003
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene