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)

P45363

- THIL_THIVI

UniProt

P45363 - THIL_THIVI

Protein

Acetyl-CoA acetyltransferase

Gene

phbA

Organism
Thiocystis violacea
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei89 – 891Acyl-thioester intermediateBy similarity
    Active sitei350 – 3501Proton acceptorPROSITE-ProRule annotation
    Active sitei380 – 3801Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA C-acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. poly-hydroxybutyrate biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    PHB biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00058; UER00101.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA acetyltransferase (EC:2.3.1.9)
    Alternative name(s):
    Acetoacetyl-CoA thiolase
    Gene namesi
    Name:phbA
    OrganismiThiocystis violacea
    Taxonomic identifieri13725 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeThiocystis

    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 – 394394Acetyl-CoA acetyltransferasePRO_0000206462Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP45363.
    SMRiP45363. Positions 4-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P45363-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDTIVIVDA GRTAIGTFGG ALSALQATDI GTTVLKALIE RTGIAPEQVS    50
    EVILGQVLTA GCGQNPARQT TLMAGLPHTV PAMTINKVCG SGLKAVHLAM 100
    QAVACGDAEI VIAGGQESMS QSSHVLPRSR EGQRMGDWPM KDTMIVDGLW 150
    DAFNQCHMGV TAENIAKKYA FTREAQDAFA AASQQKAEAA IQSGRFADEI 200
    IPVSIPQRKG DPLVFDTDEF PRPGTTAETL GRLRPAFDKQ GTVTAGNASG 250
    INDGAAMVVV MKESKAKELG LTPMARLVAF SSAGVDPAIM GTGPIPASTD 300
    CLKKAGWAPA DLDLVEANEA FAAQAMSVNQ EMGWDLSKVN VNGGAIAIGH 350
    PIGASGARVL VTLLYEMQKR DAKKGLATLC IGGGQGVALA VERL 394
    Length:394
    Mass (Da):40,897
    Last modified:November 1, 1995 - v1
    Checksum:iD51EAAE97F55E3F2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01113 Genomic DNA. Translation: AAB02860.1.
    S54369 Genomic DNA. Translation: AAC60428.2.
    PIRiB48376.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01113 Genomic DNA. Translation: AAB02860.1 .
    S54369 Genomic DNA. Translation: AAC60428.2 .
    PIRi B48376.

    3D structure databases

    ProteinModelPortali P45363.
    SMRi P45363. Positions 4-394.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00058 ; UER00101 .

    Family and domain databases

    Gene3Di 3.40.47.10. 4 hits.
    InterProi IPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view ]
    Pfami PF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMi SSF53901. SSF53901. 2 hits.
    TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEi PS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and molecular analysis of the poly(3-hydroxybutyric acid) biosynthetic genes of Thiocystis violacea."
      Liebergesell M., Steinbuechel A.
      Appl. Microbiol. Biotechnol. 38:493-501(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 2311 / DSM 208.

    Entry informationi

    Entry nameiTHIL_THIVI
    AccessioniPrimary (citable) accession number: P45363
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3