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P27253

- SCPA_ECOLI

UniProt

P27253 - SCPA_ECOLI

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Protein
Methylmalonyl-CoA mutase
Gene
scpA, sbm, yliK, b2917, JW2884
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of succinyl-CoA and methylmalonyl-CoA. Could be part of a pathway that converts succinate to propionate.2 Publications

Catalytic activityi

(R)-methylmalonyl-CoA = succinyl-CoA.2 Publications

Cofactori

Adenosylcobalamin.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi597 – 5971Cobalt (cobalamin axial ligand) By similarity

GO - Molecular functioni

  1. cobalamin binding Source: EcoCyc
  2. metal ion binding Source: UniProtKB-KW
  3. methylmalonyl-CoA mutase activity Source: EcoCyc
  4. protein binding Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA mutase (EC:5.4.99.2)
Short name:
MCM
Gene namesi
Name:scpA
Synonyms:sbm, yliK
Ordered Locus Names:b2917, JW2884
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11444. scpA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 714714Methylmalonyl-CoA mutase
PRO_0000194277Add
BLAST

Proteomic databases

PaxDbiP27253.
PRIDEiP27253.

Expressioni

Gene expression databases

GenevestigatoriP27253.

Interactioni

Subunit structurei

Homodimer. Interacts with ArgK.1 Publication

Protein-protein interaction databases

IntActiP27253. 6 interactions.
STRINGi511145.b2917.

Structurei

3D structure databases

ProteinModelPortaliP27253.
SMRiP27253. Positions 28-701.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini584 – 714131B12-binding
Add
BLAST

Sequence similaritiesi

Contains 1 B12-binding domain.

Phylogenomic databases

eggNOGiCOG2185.
HOGENOMiHOG000003917.
KOiK01847.
OMAiSIYDMRQ.
OrthoDBiEOG6423BW.
PhylomeDBiP27253.

Family and domain databases

Gene3Di3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProiIPR006159. 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]
PfamiPF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
SUPFAMiSSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27253-1 [UniParc]FASTAAdd to Basket

« Hide

MSNVQEWQQL ANKELSRREK TVDSLVHQTA EGIAIKPLYT EADLDNLEVT    50
GTLPGLPPYV RGPRATMYTA QPWTIRQYAG FSTAKESNAF YRRNLAAGQK 100
GLSVAFDLAT HRGYDSDNPR VAGDVGKAGV AIDTVEDMKV LFDQIPLDKM 150
SVSMTMNGAV LPVLAFYIVA AEEQGVTPDK LTGTIQNDIL KEYLCRNTYI 200
YPPKPSMRII ADIIAWCSGN MPRFNTISIS GYHMGEAGAN CVQQVAFTLA 250
DGIEYIKAAI SAGLKIDDFA PRLSFFFGIG MDLFMNVAML RAARYLWSEA 300
VSGFGAQDPK SLALRTHCQT SGWSLTEQDP YNNVIRTTIE ALAATLGGTQ 350
SLHTNAFDEA LGLPTDFSAR IARNTQIIIQ EESELCRTVD PLAGSYYIES 400
LTDQIVKQAR AIIQQIDEAG GMAKAIEAGL PKRMIEEASA REQSLIDQGK 450
RVIVGVNKYK LDHEDETDVL EIDNVMVRNE QIASLERIRA TRDDAAVTAA 500
LNALTHAAQH NENLLAAAVN AARVRATLGE ISDALEVAFD RYLVPSQCVT 550
GVIAQSYHQS EKSASEFDAI VAQTEQFLAD NGRRPRILIA KMGQDGHDRG 600
AKVIASAYSD LGFDVDLSPM FSTPEEIARL AVENDVHVVG ASSLAAGHKT 650
LIPELVEALK KWGREDICVV AGGVIPPQDY AFLQERGVAA IYGPGTPMLD 700
SVRDVLNLIS QHHD 714
Length:714
Mass (Da):77,871
Last modified:August 29, 2003 - v2
Checksum:i65222F5EB2F4633A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3561A → V in CAA47311. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66836 Genomic DNA. Translation: CAA47311.1.
U28377 Genomic DNA. Translation: AAA69084.1.
U00096 Genomic DNA. Translation: AAC75954.1.
AP009048 Genomic DNA. Translation: BAE76981.1.
PIRiD65076.
RefSeqiNP_417392.1. NC_000913.3.
YP_491117.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75954; AAC75954; b2917.
BAE76981; BAE76981; BAE76981.
GeneIDi12933336.
945576.
KEGGiecj:Y75_p2848.
eco:b2917.
PATRICi32121248. VBIEscCol129921_3012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66836 Genomic DNA. Translation: CAA47311.1 .
U28377 Genomic DNA. Translation: AAA69084.1 .
U00096 Genomic DNA. Translation: AAC75954.1 .
AP009048 Genomic DNA. Translation: BAE76981.1 .
PIRi D65076.
RefSeqi NP_417392.1. NC_000913.3.
YP_491117.1. NC_007779.1.

3D structure databases

ProteinModelPortali P27253.
SMRi P27253. Positions 28-701.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P27253. 6 interactions.
STRINGi 511145.b2917.

Proteomic databases

PaxDbi P27253.
PRIDEi P27253.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75954 ; AAC75954 ; b2917 .
BAE76981 ; BAE76981 ; BAE76981 .
GeneIDi 12933336.
945576.
KEGGi ecj:Y75_p2848.
eco:b2917.
PATRICi 32121248. VBIEscCol129921_3012.

Organism-specific databases

EchoBASEi EB1414.
EcoGenei EG11444. scpA.

Phylogenomic databases

eggNOGi COG2185.
HOGENOMi HOG000003917.
KOi K01847.
OMAi SIYDMRQ.
OrthoDBi EOG6423BW.
PhylomeDBi P27253.

Enzyme and pathway databases

BioCyci EcoCyc:METHYLMALONYL-COA-MUT-MONOMER.
ECOL316407:JW2884-MONOMER.
MetaCyc:METHYLMALONYL-COA-MUT-MONOMER.

Miscellaneous databases

PROi P27253.

Gene expression databases

Genevestigatori P27253.

Family and domain databases

Gene3Di 3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProi IPR006159. 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 ]
Pfami PF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view ]
SUPFAMi SSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsi TIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.
PROSITEi PS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiSCPA_ECOLI
AccessioniPrimary (citable) accession number: P27253
Secondary accession number(s): Q2M9S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 29, 2003
Last modified: June 11, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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