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Q01103

- PCAI_PSEPU

UniProt

Q01103 - PCAI_PSEPU

Protein

3-oxoadipate CoA-transferase subunit A

Gene

pcaI

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA.

    Pathwayi

    GO - Molecular functioni

    1. 3-oxoadipate CoA-transferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. beta-ketoadipate pathway Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3190.
    RETL1328306-WGS:GSTH-6059-MONOMER.
    UniPathwayiUPA00157; UER00262.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-oxoadipate CoA-transferase subunit A (EC:2.8.3.6)
    Alternative name(s):
    Beta-ketoadipate:succinyl-CoA transferase subunit A
    Gene namesi
    Name:pcaI
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2312313-oxoadipate CoA-transferase subunit APRO_0000157907Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01103.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 317CoA-bindingSequence Analysis

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR012792. 3-oxoacid_CoA-transf_A.
    IPR004165. CoA_trans_fam_I.
    IPR004163. CoA_transf_BS.
    [Graphical view]
    PANTHERiPTHR13707. PTHR13707. 1 hit.
    PfamiPF01144. CoA_trans. 1 hit.
    [Graphical view]
    SMARTiSM00882. CoA_trans. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02429. pcaI_scoA_fam. 1 hit.
    PROSITEiPS01273. COA_TRANSF_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q01103-1 [UniParc]FASTAAdd to Basket

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    MINKTYESIA SAVEGITDGS TIMVGGFGTA GMPSELIDGL IATGARDLTI    50
    ISNNAGNGEI GLAALLMAGS VRKVVCSFPR QSDSYVFDEL YRAGKIELEV 100
    VPQGNLAERI AAAGSGIGAF FSPTGYGTLL AEGKETREID GRMYVLEMPL 150
    HADFALIKAH KGDRWGNLTY RKAARNFGPI MAMAAKTAIA QVDQVVELGE 200
    LDPEHIITPG IFVQRVVAVS GAAASSIAKA I 231
    Length:231
    Mass (Da):24,234
    Last modified:November 1, 1995 - v2
    Checksum:iB5071507AC6A442C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88763 Genomic DNA. Translation: AAA25922.1.
    PIRiA42985.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88763 Genomic DNA. Translation: AAA25922.1 .
    PIRi A42985.

    3D structure databases

    ProteinModelPortali Q01103.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00157 ; UER00262 .
    BioCyci MetaCyc:MONOMER-3190.
    RETL1328306-WGS:GSTH-6059-MONOMER.

    Family and domain databases

    InterProi IPR012792. 3-oxoacid_CoA-transf_A.
    IPR004165. CoA_trans_fam_I.
    IPR004163. CoA_transf_BS.
    [Graphical view ]
    PANTHERi PTHR13707. PTHR13707. 1 hit.
    Pfami PF01144. CoA_trans. 1 hit.
    [Graphical view ]
    SMARTi SM00882. CoA_trans. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02429. pcaI_scoA_fam. 1 hit.
    PROSITEi PS01273. COA_TRANSF_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida."
      Parales R.E., Harwood C.S.
      J. Bacteriol. 174:4657-4666(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: PRS2000.
    2. "Evolutionarily homologous alpha 2 beta 2 oligomeric structures in beta-ketoadipate succinyl-CoA transferases from Acinetobacter calcoaceticus and Pseudomonas putida."
      Yeh W.-K., Ornston L.N.
      J. Biol. Chem. 256:1565-1569(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-6.

    Entry informationi

    Entry nameiPCAI_PSEPU
    AccessioniPrimary (citable) accession number: Q01103
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 63 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

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3