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P31572

- CAIB_ECOLI

UniProt

P31572 - CAIB_ECOLI

Protein

L-carnitine CoA-transferase

Gene

caiB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA.1 Publication

    Catalytic activityi

    (E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA.
    4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei97 – 971Coenzyme A1 Publication
    Binding sitei104 – 1041Coenzyme A1 Publication
    Active sitei169 – 1691Nucleophile

    GO - Molecular functioni

    1. carnitine dehydratase activity Source: EcoliWiki
    2. CoA-transferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. carnitine catabolic process Source: EcoliWiki

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:CARNDEHYDRA-MONOMER.
    ECOL316407:JW0037-MONOMER.
    MetaCyc:CARNDEHYDRA-MONOMER.
    UniPathwayiUPA00117.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-carnitine CoA-transferase (EC:2.8.3.21)
    Alternative name(s):
    Crotonobetainyl-CoA:carnitine CoA-transferase
    Gene namesi
    Name:caiB
    Synonyms:yaaN
    Ordered Locus Names:b0038, JW0037
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11559. caiB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 405405L-carnitine CoA-transferasePRO_0000194708Add
    BLAST

    Proteomic databases

    PRIDEiP31572.

    Expressioni

    Inductioni

    By L-carnitine or crotonobetaine.

    Gene expression databases

    GenevestigatoriP31572.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP31572. 12 interactions.
    STRINGi511145.b0038.

    Structurei

    Secondary structure

    1
    405
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni11 – 144
    Beta strandi16 – 205
    Helixi25 – 3511
    Beta strandi39 – 446
    Beta strandi46 – 483
    Helixi51 – 544
    Beta strandi55 – 573
    Helixi58 – 625
    Turni63 – 653
    Beta strandi67 – 715
    Beta strandi73 – 753
    Helixi76 – 8611
    Beta strandi90 – 956
    Beta strandi97 – 993
    Helixi100 – 1034
    Helixi108 – 1147
    Beta strandi119 – 1268
    Beta strandi128 – 1303
    Turni132 – 1365
    Helixi141 – 1477
    Helixi151 – 1533
    Beta strandi154 – 1563
    Turni164 – 1663
    Helixi167 – 19024
    Beta strandi194 – 1996
    Helixi200 – 2078
    Helixi209 – 2168
    Beta strandi231 – 2333
    Beta strandi236 – 2416
    Beta strandi244 – 2496
    Helixi253 – 26311
    Helixi266 – 2683
    Beta strandi271 – 2744
    Turni283 – 2853
    Helixi289 – 30113
    Helixi305 – 31410
    Beta strandi318 – 3214
    Helixi325 – 3273
    Helixi332 – 3376
    Beta strandi340 – 3445
    Beta strandi350 – 3545
    Beta strandi361 – 3633
    Turni374 – 3774
    Helixi378 – 3847
    Helixi389 – 3979
    Beta strandi400 – 4023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XA3X-ray1.85A/B2-405[»]
    1XA4X-ray1.90A/B2-405[»]
    1XK6X-ray1.85A/B/C/D1-405[»]
    1XK7X-ray1.60A/B/C1-405[»]
    1XVTX-ray2.30A1-405[»]
    1XVUX-ray2.40A1-405[»]
    1XVVX-ray2.40A1-405[»]
    ProteinModelPortaliP31572.
    SMRiP31572. Positions 1-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31572.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CaiB/BaiF CoA-transferase family.Curated

    Phylogenomic databases

    eggNOGiCOG1804.
    HOGENOMiHOG000219745.
    KOiK08298.
    OMAiPLRMQNV.
    OrthoDBiEOG6Q2SGC.
    PhylomeDBiP31572.

    Family and domain databases

    Gene3Di3.40.50.10540. 2 hits.
    HAMAPiMF_01050. CaiB.
    InterProiIPR003673. CoA-Trfase_fam_III.
    IPR023452. CoA-Trfase_fam_III_CaiB.
    IPR023606. CoA-Trfase_III_dom.
    [Graphical view]
    PANTHERiPTHR11837. PTHR11837. 1 hit.
    PfamiPF02515. CoA_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF89796. SSF89796. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P31572-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDHLPMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD    50
    TIRVQPNYPQ LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA 100
    FARRGITDEV LWQHNPKLVI AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY 150
    LIQNGDVDQP MPAFPYTADY FSGLTATTAA LAALHKVRET GKGESIDIAM 200
    YEVMLRMGQY FMMDYFNGGE MCPRMSKGKD PYYAGCGLYK CADGYIVMEL 250
    VGITQIEECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL 300
    ATHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT 350
    CKGPNIMPKF KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL 400
    AKVED 405
    Length:405
    Mass (Da):45,127
    Last modified:February 1, 1995 - v3
    Checksum:i75583684B4B5A2DE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti187 – 1871V → A in strain: O44:K74.
    Natural varianti302 – 3021T → A in strain: O44:K74.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67748 Genomic DNA. Translation: CAA47971.1.
    X73904 Genomic DNA. Translation: CAA52112.1.
    U00096 Genomic DNA. Translation: AAC73149.1.
    AP009048 Genomic DNA. Translation: BAB96607.1.
    PIRiS40559.
    RefSeqiNP_414580.1. NC_000913.3.
    YP_488344.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73149; AAC73149; b0038.
    BAB96607; BAB96607; BAB96607.
    GeneIDi12932590.
    948997.
    KEGGiecj:Y75_p0038.
    eco:b0038.
    PATRICi32115171. VBIEscCol129921_0037.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67748 Genomic DNA. Translation: CAA47971.1 .
    X73904 Genomic DNA. Translation: CAA52112.1 .
    U00096 Genomic DNA. Translation: AAC73149.1 .
    AP009048 Genomic DNA. Translation: BAB96607.1 .
    PIRi S40559.
    RefSeqi NP_414580.1. NC_000913.3.
    YP_488344.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XA3 X-ray 1.85 A/B 2-405 [» ]
    1XA4 X-ray 1.90 A/B 2-405 [» ]
    1XK6 X-ray 1.85 A/B/C/D 1-405 [» ]
    1XK7 X-ray 1.60 A/B/C 1-405 [» ]
    1XVT X-ray 2.30 A 1-405 [» ]
    1XVU X-ray 2.40 A 1-405 [» ]
    1XVV X-ray 2.40 A 1-405 [» ]
    ProteinModelPortali P31572.
    SMRi P31572. Positions 1-405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P31572. 12 interactions.
    STRINGi 511145.b0038.

    Proteomic databases

    PRIDEi P31572.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73149 ; AAC73149 ; b0038 .
    BAB96607 ; BAB96607 ; BAB96607 .
    GeneIDi 12932590.
    948997.
    KEGGi ecj:Y75_p0038.
    eco:b0038.
    PATRICi 32115171. VBIEscCol129921_0037.

    Organism-specific databases

    EchoBASEi EB1520.
    EcoGenei EG11559. caiB.

    Phylogenomic databases

    eggNOGi COG1804.
    HOGENOMi HOG000219745.
    KOi K08298.
    OMAi PLRMQNV.
    OrthoDBi EOG6Q2SGC.
    PhylomeDBi P31572.

    Enzyme and pathway databases

    UniPathwayi UPA00117 .
    BioCyci EcoCyc:CARNDEHYDRA-MONOMER.
    ECOL316407:JW0037-MONOMER.
    MetaCyc:CARNDEHYDRA-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P31572.
    PROi P31572.

    Gene expression databases

    Genevestigatori P31572.

    Family and domain databases

    Gene3Di 3.40.50.10540. 2 hits.
    HAMAPi MF_01050. CaiB.
    InterProi IPR003673. CoA-Trfase_fam_III.
    IPR023452. CoA-Trfase_fam_III_CaiB.
    IPR023606. CoA-Trfase_III_dom.
    [Graphical view ]
    PANTHERi PTHR11837. PTHR11837. 1 hit.
    Pfami PF02515. CoA_transf_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF89796. SSF89796. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, nucleotide sequence, and expression of the Escherichia coli gene encoding carnitine dehydratase."
      Eichler K., Schunck W.-H., Kleber H.-P., Mandrand-Berthelot M.-A.
      J. Bacteriol. 176:2970-2975(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19.
      Strain: O44:K74.
    2. "Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli."
      Eichler K., Bourgis F., Buchet A., Kleber H.-P., Mandrand-Berthelot M.-A.
      Mol. Microbiol. 13:775-786(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: O44:K74.
    3. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli."
      Elssner T., Engemann C., Baumgart K., Kleber H.-P.
      Biochemistry 40:11140-11148(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
      Strain: O44:K74.
    7. "Metabolism of L(-)-carnitine by Enterobacteriaceae under aerobic conditions."
      Elssner T., Preusser A., Wagner U., Kleber H.-P.
      FEMS Microbiol. Lett. 174:295-301(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY UNDER AEROBIOSIS.
      Strain: ATCC 25922 / DSM 1103 / NCIB 12210 and O44:K74.
    8. "Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism."
      Stenmark P., Gurmu D., Nordlund P.
      Biochemistry 43:13996-14003(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH COENZYME A.

    Entry informationi

    Entry nameiCAIB_ECOLI
    AccessioniPrimary (citable) accession number: P31572
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Some strains of E.coli, such as ATCC 25922, can metabolize carnitine under aerobiosis.

    Caution

    Was originally thought to be an L-carnitine dehydratase.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3