Acetyl-CoA acetyltransferase
Details
- Name
- Acetyl-CoA acetyltransferase
- Synonyms
- 2.3.1.9
- Acetoacetyl-CoA thiolase
- Gene Name
- phbA
- Organism
- Zoogloea ramigera
- Amino acid sequence
>lcl|BSEQ0010998|Acetyl-CoA acetyltransferase MSTPSIVIASARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPA GEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMS MAPHCAHLAGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAENVAKQWQLSRDEQDAFAV ASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGT VTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKAL ERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNT LLFEMKRRGARKGLATLCIGGGMGVAMCIESL
- Number of residues
- 392
- Molecular Weight
- 40472.955
- Theoretical pI
- 6.26
- GO Classification
- Functionsacetyl-CoA C-acetyltransferase activityProcessespoly-hydroxybutyrate biosynthetic processComponentscytoplasm
- General Function
- Acetyl-coa c-acetyltransferase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0002822|1176 bp ATGAGCACCCCGTCCATCGTCATCGCCAGCGCCCGCACCGCGGTCGGTTCCTTCAACGGC GCTTTCGCCAACACGCCCGCCCATGAACTCGGGGCGACCGTGATTTCGGCGGTTCTCGAG CGCGCGGGCGTTGCGGCGGGCGAGGTGAACGAGGTGATTCTCGGCCAGGTGCTGCCGGCC GGCGAAGGCCAGAACCCGGCCCGCCAGGCCGCCATGAAGGCCGGCGTGCCGCAGGAGGCG ACCGCCTGGGGCATGAACCAGCTTTGCGGCTCGGGCCTGCGCGCCGTCGCGCTCGGCATG CAGCAGATCGCCACGGGCGATGCGAGCATCATCGTCGCCGGCGGCATGGAATCCATGTCC ATGGCCCCGCATTGCGCGCATCTGGCCGGCGTGAAGATGGGCGATTTCAAGATGATCGAC ACGATGATCAAGGACGGCCTGACCGACGCCTTCTACGGCTACCACATGGGCACGACCGCC GAGAATGTCGCCAAGCAGTGGCAGCTTTCCCGCGACGAGCAGGACGCCTTCGCCGTCGCC TCGCAGAACAAGGCCGAGGCCGCCCAGAAGGACGGCCGCTTCAAGGACGAGATCGTTCCC TTCATCGTCAAGGGCCGCAAGGGCGACATCACGGTCGATGCCGACGAATATATCCGCCAC GGCGCGACGCTCGATTCCATGGCGAAGCTCCGCCCGGCCTTCGACAAGGAAGGCACGGTG ACGGCCGGCAACGCCTCCGGCCTCAATGACGGCGCGGCCGCGGCCCTCCTGATGAGCGAA GCGGAAGCCTCGCGCCGCGGCATCCAGCCGCTCGGCCGCATCGTTTCCTGGGCGACGGTC GGCGTCGATCCCAAGGTCATGGGCACCGGCCCGATCCCGGCCTCCCGCAAGGCGCTCGAG CGCGCCGGCTGGAAGATCGGCGATCTCGACCTCGTGGAAGCCAACGAAGCCTTCGCGGCG CAGGCCTGCGCGGTCAACAAGGACCTCGGCTGGGATCCGTCCATCGTCAACGTCAACGGC GGTGCCATCGCCATCGGCCACCCGATCGGCGCGTCCGGCGCCCGCATCCTCAACACGCTC CTCTTCGAGATGAAGCGTCGCGGCGCCCGCAAGGGTCTCGCCACGCTCTGCATCGGCGGC GGCATGGGCGTGGCGATGTGCATCGAGAGCCTTTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P07097 UniProtKB Entry Name THIL_ZOORA GenBank Protein ID 155618 GenBank Gene ID J02631 - General References
- Peoples OP, Masamune S, Walsh CT, Sinskey AJ: Biosynthetic thiolase from Zoogloea ramigera. III. Isolation and characterization of the structural gene. J Biol Chem. 1987 Jan 5;262(1):97-102. [Article]
- Peoples OP, Sinskey AJ: Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase. J Biol Chem. 1989 Sep 15;264(26):15293-7. [Article]
- Palmer MA, Differding E, Gamboni R, Williams SF, Peoples OP, Walsh CT, Sinskey AJ, Masamune S: Biosynthetic thiolase from Zoogloea ramigera. Evidence for a mechanism involving Cys-378 as the active site base. J Biol Chem. 1991 May 5;266(13):8369-75. [Article]
- Modis Y, Wierenga RK: Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase. J Mol Biol. 2000 Apr 14;297(5):1171-82. [Article]
- Modis Y, Wierenga RK: A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism. Structure. 1999 Oct 15;7(10):1279-90. [Article]
- Kursula P, Ojala J, Lambeir AM, Wierenga RK: The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes. Biochemistry. 2002 Dec 31;41(52):15543-56. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01915 S-Hydroxycysteine experimental unknown Details DB01992 Coenzyme A investigational, nutraceutical unknown Details DB02039 S-Acetyl-Cysteine experimental unknown Details DB02160 S-Butyryl-Cystein experimental unknown Details DB03045 Pantothenyl-Aminoethanol-Acetate Pivalic Acid experimental unknown Details DB03059 Acetoacetyl-CoA experimental unknown Details DB08328 PANTOTHENYL-AMINOETHANOL-11-PIVALIC ACID experimental unknown Details DB08408 (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate experimental unknown Details