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P07097

- THIL_ZOORA

UniProt

P07097 - THIL_ZOORA

Protein

Acetyl-CoA acetyltransferase

Gene

phbA

Organism
Zoogloea ramigera
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      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 intermediate
    Active sitei348 – 3481Proton acceptor
    Active sitei378 – 3781Proton acceptor

    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

    BioCyciRETL1328306-WGS:GSTH-4110-MONOMER.
    RETL1328306-WGS:GSTH-6457-MONOMER.
    SABIO-RKP07097.
    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
    OrganismiZoogloea ramigera
    Taxonomic identifieri350 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeZoogloea

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641Q → A: Slightly lower activity. 1 Publication
    Mutagenesisi89 – 891C → A: Loss of activity. 1 Publication
    Mutagenesisi378 – 3781C → G: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 392391Acetyl-CoA acetyltransferasePRO_0000206463Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    392
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 127
    Turni21 – 244
    Helixi27 – 4216
    Helixi46 – 483
    Beta strandi51 – 555
    Helixi66 – 738
    Beta strandi80 – 867
    Helixi88 – 903
    Helixi91 – 10414
    Beta strandi111 – 1199
    Beta strandi124 – 1263
    Beta strandi133 – 1353
    Beta strandi137 – 1415
    Helixi142 – 1476
    Turni151 – 1533
    Helixi157 – 16812
    Helixi172 – 19221
    Turni193 – 1986
    Beta strandi202 – 2043
    Beta strandi211 – 2133
    Helixi225 – 2295
    Beta strandi233 – 2353
    Beta strandi243 – 2464
    Beta strandi250 – 26011
    Helixi261 – 2677
    Beta strandi272 – 28211
    Helixi285 – 2906
    Helixi292 – 30312
    Helixi307 – 3093
    Beta strandi311 – 3155
    Helixi320 – 33011
    Helixi334 – 3363
    Helixi343 – 3464
    Helixi350 – 3523
    Helixi353 – 36816
    Beta strandi371 – 3799
    Turni380 – 3823
    Beta strandi383 – 3908

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DLUX-ray2.25A/B/C/D5-392[»]
    1DLVX-ray2.29A/B/C/D5-392[»]
    1DM3X-ray2.00A/B/C/D5-392[»]
    1M1OX-ray1.95A/B/C/D2-392[»]
    1M1TX-ray1.94A/B/C/D2-392[»]
    1M3KX-ray1.70A/B/C/D2-392[»]
    1M3ZX-ray1.87A/B/C/D2-392[»]
    1M4SX-ray1.87A/B/C/D2-392[»]
    1M4TX-ray1.77A/B/C/D2-392[»]
    1NL7X-ray1.90A/B/C/D2-392[»]
    1OU6X-ray2.07A/B/C/D2-392[»]
    1QFLX-ray1.92A/B/C/D5-392[»]
    2VTZX-ray2.30A/B/C/D2-392[»]
    2VU0X-ray1.87A/B/C/D2-392[»]
    2VU1X-ray1.51A/B/C/D12-392[»]
    2VU2X-ray2.65A/B/C/D2-392[»]
    2WKTX-ray2.00A/B/C/D2-392[»]
    2WKUX-ray2.30A/B/C/D2-392[»]
    2WKVX-ray2.50A/B/C/D2-392[»]
    2WL4X-ray1.80A/B/C/D2-392[»]
    2WL5X-ray1.80A/B/C/D2-392[»]
    2WL6X-ray2.98A/B/C/D2-392[»]
    ProteinModelPortaliP07097.
    SMRiP07097. Positions 5-392.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07097.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P07097-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPSIVIAS ARTAVGSFNG AFANTPAHEL GATVISAVLE RAGVAAGEVN    50
    EVILGQVLPA GEGQNPARQA AMKAGVPQEA TAWGMNQLCG SGLRAVALGM 100
    QQIATGDASI IVAGGMESMS MAPHCAHLAG GVKMGDFKMI DTMIKDGLTD 150
    AFYGYHMGTT AENVAKQWQL SRDEQDAFAV ASQNKAEAAQ KDGRFKDEIV 200
    PFIVKGRKGD ITVDADEYIR HGATLDSMAK LRPAFDKEGT VTAGNASGLN 250
    DGAAAALLMS EAEASRRGIQ PLGRIVSWAT VGVDPKVMGT GPIPASRKAL 300
    ERAGWKIGDL DLVEANEAFA AQACAVNKDL GWDPSIVNVN GGAIAIGHPI 350
    GASGARILNT LLFEMKRRGA RKGLATLCIG GGMGVAMCIE SL 392
    Length:392
    Mass (Da):40,473
    Last modified:January 23, 2007 - v4
    Checksum:i88A6298751A42B7E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02631 Genomic DNA. Translation: AAA27706.1. Sequence problems.
    PIRiA26121. XXGZAC.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02631 Genomic DNA. Translation: AAA27706.1 . Sequence problems.
    PIRi A26121. XXGZAC.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DLU X-ray 2.25 A/B/C/D 5-392 [» ]
    1DLV X-ray 2.29 A/B/C/D 5-392 [» ]
    1DM3 X-ray 2.00 A/B/C/D 5-392 [» ]
    1M1O X-ray 1.95 A/B/C/D 2-392 [» ]
    1M1T X-ray 1.94 A/B/C/D 2-392 [» ]
    1M3K X-ray 1.70 A/B/C/D 2-392 [» ]
    1M3Z X-ray 1.87 A/B/C/D 2-392 [» ]
    1M4S X-ray 1.87 A/B/C/D 2-392 [» ]
    1M4T X-ray 1.77 A/B/C/D 2-392 [» ]
    1NL7 X-ray 1.90 A/B/C/D 2-392 [» ]
    1OU6 X-ray 2.07 A/B/C/D 2-392 [» ]
    1QFL X-ray 1.92 A/B/C/D 5-392 [» ]
    2VTZ X-ray 2.30 A/B/C/D 2-392 [» ]
    2VU0 X-ray 1.87 A/B/C/D 2-392 [» ]
    2VU1 X-ray 1.51 A/B/C/D 12-392 [» ]
    2VU2 X-ray 2.65 A/B/C/D 2-392 [» ]
    2WKT X-ray 2.00 A/B/C/D 2-392 [» ]
    2WKU X-ray 2.30 A/B/C/D 2-392 [» ]
    2WKV X-ray 2.50 A/B/C/D 2-392 [» ]
    2WL4 X-ray 1.80 A/B/C/D 2-392 [» ]
    2WL5 X-ray 1.80 A/B/C/D 2-392 [» ]
    2WL6 X-ray 2.98 A/B/C/D 2-392 [» ]
    ProteinModelPortali P07097.
    SMRi P07097. Positions 5-392.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00058 ; UER00101 .
    BioCyci RETL1328306-WGS:GSTH-4110-MONOMER.
    RETL1328306-WGS:GSTH-6457-MONOMER.
    SABIO-RK P07097.

    Miscellaneous databases

    EvolutionaryTracei P07097.

    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. "Biosynthetic thiolase from Zoogloea ramigera. III. Isolation and characterization of the structural gene."
      Peoples O.P., Masamune S., Walsh C.T., Sinskey A.J.
      J. Biol. Chem. 262:97-102(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 19623 / I-16-M / NCIB 10340 / NCTC 10482.
    2. "Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase."
      Peoples O.P., Sinskey A.J.
      J. Biol. Chem. 264:15293-15297(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 131.
    3. "Biosynthetic thiolase from Zoogloea ramigera. Evidence for a mechanism involving Cys-378 as the active site base."
      Palmer M.A.J., Differding E., Gamboni R., Williams S.F., Peoples O.P., Walsh C.T., Sinskey S.J., Masamune S.
      J. Biol. Chem. 266:8369-8375(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-378.
    4. "Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase."
      Modis Y., Wierenga R.K.
      J. Mol. Biol. 297:1171-1182(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
    5. "A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism."
      Modis Y., Wierenga R.K.
      Structure 7:1279-1290(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF THE THIOESTER INTERMEDIATE AND OF COMPLEX WITH SUBSTRATE.
    6. "The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes."
      Kursula P., Ojala J., Lambeir A.-M., Wierenga R.K.
      Biochemistry 41:15543-15556(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF THE THIOESTER INTERMEDIATE; OF COMPLEX WITH SUBSTRATE AND OF MUTANTS ALA-64 AND ALA-89, MUTAGENESIS OF GLN-64 AND CYS-89.

    Entry informationi

    Entry nameiTHIL_ZOORA
    AccessioniPrimary (citable) accession number: P07097
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

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

    External Data

    Dasty 3