Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27253

- SCPA_ECOLI

UniProt

P27253 - SCPA_ECOLI

Protein

Methylmalonyl-CoA mutase

Gene

scpA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (29 Aug 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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 mutasePRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini584 – 714131B12-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the methylmalonyl-CoA mutase family.Curated
    Contains 1 B12-binding domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti356 – 3561A → V in CAA47311. (PubMed:1355087)Curated

    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

    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: October 1, 2014
    This is version 117 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