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P52045

- SCPB_ECOLI

UniProt

P52045 - SCPB_ECOLI

Protein

Methylmalonyl-CoA decarboxylase

Gene

scpB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the decarboxylation of methylmalonyl-CoA to propionyl-CoA. Could be part of a pathway that converts succinate to propionate.1 Publication

    Catalytic activityi

    (S)-methylmalonyl-CoA = propanoyl-CoA + CO2.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei110 – 1101Substrate; via amide nitrogen1 Publication
    Binding sitei132 – 1321Substrate1 Publication
    Binding sitei253 – 2531Substrate1 Publication

    GO - Molecular functioni

    1. carboxy-lyase activity Source: UniProtKB
    2. methylmalonyl-CoA decarboxylase activity Source: EcoCyc

    Keywords - Molecular functioni

    Lyase

    Enzyme and pathway databases

    BioCyciEcoCyc:G7516-MONOMER.
    ECOL316407:JW2886-MONOMER.
    MetaCyc:G7516-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylmalonyl-CoA decarboxylase (EC:4.1.1.41)
    Short name:
    MMCD
    Alternative name(s):
    Transcarboxylase
    Gene namesi
    Name:scpB
    Synonyms:mmcD, ygfG
    Ordered Locus Names:b2919, JW2886
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12972. scpB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261Methylmalonyl-CoA decarboxylasePRO_0000109355Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP52045.

    Interactioni

    Subunit structurei

    Dimer of homotrimers.1 Publication

    Protein-protein interaction databases

    STRINGi511145.b2919.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 118
    Beta strandi14 – 196
    Helixi22 – 243
    Helixi30 – 4213
    Beta strandi50 – 545
    Beta strandi60 – 634
    Helixi68 – 703
    Beta strandi74 – 763
    Beta strandi81 – 833
    Helixi84 – 9411
    Beta strandi99 – 1035
    Beta strandi105 – 1084
    Helixi110 – 1178
    Beta strandi118 – 1247
    Beta strandi128 – 1303
    Helixi133 – 1364
    Helixi142 – 1465
    Beta strandi149 – 1524
    Helixi154 – 16310
    Helixi169 – 1746
    Beta strandi179 – 1824
    Helixi184 – 1863
    Helixi187 – 19812
    Helixi203 – 21816
    Helixi224 – 23815
    Helixi241 – 25111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EF8X-ray1.85A/B/C1-261[»]
    1EF9X-ray2.70A1-261[»]
    ProteinModelPortaliP52045.
    SMRiP52045. Positions 1-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52045.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 685Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1024.
    HOGENOMiHOG000027939.
    KOiK11264.
    OMAiKRKPHFV.
    OrthoDBiEOG6M9F0M.
    PhylomeDBiP52045.

    Family and domain databases

    Gene3Di1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P52045-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSYQYVNVVT INKVAVIEFN YGRKLNALSK VFIDDLMQAL SDLNRPEIRC    50
    IILRAPSGSK VFSAGHDIHE LPSGGRDPLS YDDPLRQITR MIQKFPKPII 100
    SMVEGSVWGG AFEMIMSSDL IIAASTSTFS MTPVNLGVPY NLVGIHNLTR 150
    DAGFHIVKEL IFTASPITAQ RALAVGILNH VVEVEELEDF TLQMAHHISE 200
    KAPLAIAVIK EELRVLGEAH TMNSDEFERI QGMRRAVYDS EDYQEGMNAF 250
    LEKRKPNFVG H 261
    Length:261
    Mass (Da):29,173
    Last modified:October 1, 1996 - v1
    Checksum:iB6A8A13EC2C2EBE0
    GO

    Sequence cautioni

    The sequence AAA69086.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28377 Genomic DNA. Translation: AAA69086.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC75956.2.
    AP009048 Genomic DNA. Translation: BAE76983.1.
    RefSeqiNP_417394.4. NC_000913.3.
    YP_491119.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75956; AAC75956; b2919.
    BAE76983; BAE76983; BAE76983.
    GeneIDi12930444.
    947408.
    KEGGiecj:Y75_p2850.
    eco:b2919.
    PATRICi32121252. VBIEscCol129921_3014.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28377 Genomic DNA. Translation: AAA69086.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC75956.2 .
    AP009048 Genomic DNA. Translation: BAE76983.1 .
    RefSeqi NP_417394.4. NC_000913.3.
    YP_491119.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EF8 X-ray 1.85 A/B/C 1-261 [» ]
    1EF9 X-ray 2.70 A 1-261 [» ]
    ProteinModelPortali P52045.
    SMRi P52045. Positions 1-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 511145.b2919.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75956 ; AAC75956 ; b2919 .
    BAE76983 ; BAE76983 ; BAE76983 .
    GeneIDi 12930444.
    947408.
    KEGGi ecj:Y75_p2850.
    eco:b2919.
    PATRICi 32121252. VBIEscCol129921_3014.

    Organism-specific databases

    EchoBASEi EB2799.
    EcoGenei EG12972. scpB.

    Phylogenomic databases

    eggNOGi COG1024.
    HOGENOMi HOG000027939.
    KOi K11264.
    OMAi KRKPHFV.
    OrthoDBi EOG6M9F0M.
    PhylomeDBi P52045.

    Enzyme and pathway databases

    BioCyci EcoCyc:G7516-MONOMER.
    ECOL316407:JW2886-MONOMER.
    MetaCyc:G7516-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P52045.
    PROi P52045.

    Gene expression databases

    Genevestigatori P52045.

    Family and domain databases

    Gene3Di 1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view ]
    Pfami PF00378. ECH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52096. SSF52096. 1 hit.
    PROSITEi PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. "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.
    3. "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.
      Strain: K12 / MG1655 / ATCC 47076.
    4. "New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli."
      Benning M.M., Haller T., Gerlt J.A., Holden H.M.
      Biochemistry 39:4630-4639(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.

    Entry informationi

    Entry nameiSCPB_ECOLI
    AccessioniPrimary (citable) accession number: P52045
    Secondary accession number(s): P76643, Q2M9S3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3