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P00484

- CAT3_ECOLX

UniProt

P00484 - CAT3_ECOLX

Protein

Chloramphenicol acetyltransferase 3

Gene

cat3

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    This enzyme is an effector of chloramphenicol resistance in bacteria.

    Catalytic activityi

    Acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei189 – 1891Proton acceptor

    GO - Molecular functioni

    1. chloramphenicol O-acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Antibiotic resistance

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chloramphenicol acetyltransferase 3 (EC:2.3.1.28)
    Alternative name(s):
    Chloramphenicol acetyltransferase III
    Short name:
    CAT-III
    Gene namesi
    Name:cat3
    Encoded oniPlasmid IncK R3870 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 213213Chloramphenicol acetyltransferase 3PRO_0000165877Add
    BLAST

    Proteomic databases

    PRIDEiP00484.

    Interactioni

    Subunit structurei

    Homotrimer.

    Structurei

    Secondary structure

    1
    213
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Helixi8 – 103
    Helixi14 – 229
    Beta strandi27 – 359
    Helixi37 – 448
    Helixi50 – 6213
    Helixi66 – 683
    Beta strandi69 – 735
    Beta strandi76 – 816
    Beta strandi84 – 918
    Turni92 – 954
    Beta strandi96 – 1016
    Helixi108 – 12215
    Beta strandi127 – 1293
    Beta strandi136 – 1449
    Beta strandi166 – 1705
    Beta strandi173 – 1753
    Beta strandi178 – 18811
    Turni189 – 1913
    Helixi194 – 20815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CIAX-ray2.50A1-213[»]
    1CLAX-ray2.34A1-213[»]
    1QCAX-ray2.20A1-213[»]
    2CLAX-ray2.35A1-213[»]
    3CLAX-ray1.75A1-213[»]
    4CLAX-ray2.00A1-213[»]
    ProteinModelPortaliP00484.
    SMRiP00484. Positions 1-213.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00484.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    InterProiIPR023213. CAT-like_dom.
    IPR018372. Chloramphenicol_AcTrfase_AS.
    IPR001707. Cmp_AcTrfase.
    [Graphical view]
    PfamiPF00302. CAT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000440. CAT. 1 hit.
    ProDomiPD002660. Cmp_AcTrfase. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM01059. CAT. 1 hit.
    [Graphical view]
    PROSITEiPS00100. CAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00484-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNYTKFDVKN WVRREHFEFY RHRLPCGFSL TSKIDITTLK KSLDDSAYKF    50
    YPVMIYLIAQ AVNQFDELRM AIKDDELIVW DSVDPQFTVF HQETETFSAL 100
    SCPYSSDIDQ FMVNYLSVME RYKSDTKLFP QGVTPENHLN ISALPWVNFD 150
    SFNLNVANFT DYFAPIITMA KYQQEGDRLL LPLSVQVHHA VCDGFHVARF 200
    INRLQELCNS KLK 213
    Length:213
    Mass (Da):24,994
    Last modified:August 1, 1988 - v1
    Checksum:i4A96839AB590CB1D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07848 Genomic DNA. Translation: CAA30695.1.
    PIRiA00567. XXECC3.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07848 Genomic DNA. Translation: CAA30695.1 .
    PIRi A00567. XXECC3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CIA X-ray 2.50 A 1-213 [» ]
    1CLA X-ray 2.34 A 1-213 [» ]
    1QCA X-ray 2.20 A 1-213 [» ]
    2CLA X-ray 2.35 A 1-213 [» ]
    3CLA X-ray 1.75 A 1-213 [» ]
    4CLA X-ray 2.00 A 1-213 [» ]
    ProteinModelPortali P00484.
    SMRi P00484. Positions 1-213.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00446. Chloramphenicol.
    DB02703. Fusidic Acid.

    Proteomic databases

    PRIDEi P00484.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00484.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    InterProi IPR023213. CAT-like_dom.
    IPR018372. Chloramphenicol_AcTrfase_AS.
    IPR001707. Cmp_AcTrfase.
    [Graphical view ]
    Pfami PF00302. CAT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000440. CAT. 1 hit.
    ProDomi PD002660. Cmp_AcTrfase. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM01059. CAT. 1 hit.
    [Graphical view ]
    PROSITEi PS00100. CAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence analysis and overexpression of the gene encoding a type III chloramphenicol acetyltransferase."
      Murray I.A., Hawkins A.R., Keyte J.W., Shaw W.V.
      Biochem. J. 252:173-179(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. "Structure of chloramphenicol acetyltransferase at 1.75-A resolution."
      Leslie A.G.W., Moody P.C.E., Shaw W.V.
      Proc. Natl. Acad. Sci. U.S.A. 85:4133-4137(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
    3. "Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75-A resolution."
      Leslie A.G.W.
      J. Mol. Biol. 213:167-186(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

    Entry informationi

    Entry nameiCAT3_ECOLX
    AccessioniPrimary (citable) accession number: P00484
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 93 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, Direct protein sequencing, Plasmid

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3