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P45369

- THIL_ALLVD

UniProt

P45369 - THIL_ALLVD

Protein

Acetyl-CoA acetyltransferase

Gene

phbA

Organism
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      Previous versions | rss
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    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

    BioCyciAVIN572477:GCJK-63-MONOMER.
    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
    Ordered Locus Names:Alvin_0063
    OrganismiAllochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum)
    Taxonomic identifieri572477 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeAllochromatium
    ProteomesiUP000001441: Chromosome

    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_0000206419Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP45369.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000012238.
    KOiK00626.

    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.

    P45369-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNENIVIVDA GRSAIGTFSG SLSSLSATEI GTAVLKGLLA RTGLAPEQID    50
    EVILGQVLTA GVGQNPARQT TLKAGLPHSV PAMTINKVCG SGLKAVHLAM 100
    QAIACGDADI VIAGGQESMS QSSHVLPRSR DGQRMGDWSM KDTMIVDGLW 150
    DAFNNYHMGT TAENIAQKYG FTREQQDAFA AASQQKTEAA QKAGRFQDEI 200
    IPIEIPQRKG DPKVFDADEF PRHGTTAESL GKLRPAFSRD GSVTAGNASG 250
    INDGAAMVVV MKESKAKELG LKPMARLVAF ASAGVDPAIM GTGPIPASTK 300
    CLEKAGWTPA DLDLIEANEA FAAQAMSVNQ DMGWDLSKVN VNGGAIAIGH 350
    PIGASGARVL VTLLYEMQKR DAKKGLATLC IGGGQGVALA VERM 394
    Length:394
    Mass (Da):41,129
    Last modified:June 15, 2010 - v2
    Checksum:i8AECC7EB26B29344
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21N → S in AAA23322. (PubMed:1396692)Curated
    Sequence conflicti19 – 191S → G in AAA23322. (PubMed:1396692)Curated
    Sequence conflicti73 – 731K → H in AAA23322. (PubMed:1396692)Curated
    Sequence conflicti239 – 2391R → K in AAA23322. (PubMed:1396692)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01112 Genomic DNA. Translation: AAA23322.1.
    CP001896 Genomic DNA. Translation: ADC61035.1.
    PIRiS29276.
    RefSeqiWP_012969311.1. NC_013851.1.
    YP_003442067.1. NC_013851.1.

    Genome annotation databases

    EnsemblBacteriaiADC61035; ADC61035; Alvin_0063.
    GeneIDi8785390.
    KEGGialv:Alvin_0063.
    PATRICi31919867. VBIAllVin64954_0065.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01112 Genomic DNA. Translation: AAA23322.1 .
    CP001896 Genomic DNA. Translation: ADC61035.1 .
    PIRi S29276.
    RefSeqi WP_012969311.1. NC_013851.1.
    YP_003442067.1. NC_013851.1.

    3D structure databases

    ProteinModelPortali P45369.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADC61035 ; ADC61035 ; Alvin_0063 .
    GeneIDi 8785390.
    KEGGi alv:Alvin_0063.
    PATRICi 31919867. VBIAllVin64954_0065.

    Phylogenomic databases

    HOGENOMi HOG000012238.
    KOi K00626.

    Enzyme and pathway databases

    UniPathwayi UPA00058 ; UER00101 .
    BioCyci AVIN572477:GCJK-63-MONOMER.

    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 nucleotide sequences of genes relevant for biosynthesis of poly(3-hydroxybutyric acid) in Chromatium vinosum strain D."
      Liebergesell M., Steinbuechel A.
      Eur. J. Biochem. 209:135-150(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete sequence of chromosome of Allochromatium vinosum DSM 180."
      US DOE Joint Genome Institute
      Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., Woyke T.
      Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17899 / DSM 180 / NBRC 103801 / D.

    Entry informationi

    Entry nameiTHIL_ALLVD
    AccessioniPrimary (citable) accession number: P45369
    Secondary accession number(s): D3RUY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 87 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3