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Protein

Acetyl-CoA acetyltransferase

Gene

phaA

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of two acetyl-coA units to form acetoacetyl-CoA (PubMed:4198758). Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation (PubMed:2670936, PubMed:4198758). Also catalyzes the reverse reaction, i.e. the cleavage of acetoacetyl-CoA, and is therefore also involved in the reutilization of PHB (PubMed:4198758, PubMed:25152395).4 Publications

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation2 Publications

Enzyme regulationi

The condensation reaction is inhibited by free CoA. The cleavage reaction is characterized by substrate inhibition by acetoacetyl-CoA, which is partially relieved by free CoA.1 Publication

Kineticsi

  1. KM=390 µM for acetyl-CoA1 Publication

    pH dependencei

    Optimum pH is 7.8 for the condensation reaction and 8.1 for the reverse cleavage reaction.1 Publication

    Pathwayi: poly-(R)-3-hydroxybutanoate biosynthesis

    This protein is involved in the pathway poly-(R)-3-hydroxybutanoate biosynthesis, which is part of Biopolymer metabolism.2 Publications
    View all proteins of this organism that are known to be involved in the pathway poly-(R)-3-hydroxybutanoate biosynthesis and in Biopolymer metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei88Acyl-thioester intermediate1 Publication1
    Active sitei349Proton acceptorPROSITE-ProRule annotation1 Publication1
    Active sitei379Proton acceptorPROSITE-ProRule annotation1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionAcyltransferase, Transferase
    Biological processPHB biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13086
    UniPathwayiUPA00917

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA acetyltransferase (EC:2.3.1.91 Publication)
    Alternative name(s):
    Acetoacetyl-CoA thiolase
    Beta-ketothiolase1 Publication
    Gene namesi
    Name:phaA1 Publication
    Synonyms:phbA1 Publication
    Ordered Locus Names:H16_A1438
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    Proteomesi
    • UP000008210 Componenti: Chromosome 1

    Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi88C → S: Almost complete loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi156H → A: Almost complete loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi219F → A: About 50% loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi219F → Y: 2-fold increase of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi221R → A: Almost complete loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi248S → A: About 40% loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi349H → A: Almost complete loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi379C → S: Almost complete loss of acetoacetyl-CoA thiolase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002064181 – 393Acetyl-CoA acetyltransferaseAdd BLAST393

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    STRINGi381666.H16_A1438

    Structurei

    Secondary structure

    1393
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 12Combined sources9
    Turni20 – 23Combined sources4
    Helixi26 – 41Combined sources16
    Helixi45 – 47Combined sources3
    Beta strandi50 – 54Combined sources5
    Helixi65 – 72Combined sources8
    Beta strandi81 – 85Combined sources5
    Helixi87 – 89Combined sources3
    Helixi90 – 103Combined sources14
    Beta strandi108 – 118Combined sources11
    Beta strandi123 – 125Combined sources3
    Turni126 – 130Combined sources5
    Beta strandi133 – 135Combined sources3
    Beta strandi137 – 141Combined sources5
    Helixi142 – 147Combined sources6
    Turni151 – 154Combined sources4
    Helixi157 – 168Combined sources12
    Helixi172 – 191Combined sources20
    Turni192 – 198Combined sources7
    Beta strandi202 – 204Combined sources3
    Beta strandi207 – 210Combined sources4
    Beta strandi212 – 214Combined sources3
    Helixi226 – 230Combined sources5
    Helixi244 – 246Combined sources3
    Beta strandi251 – 261Combined sources11
    Helixi262 – 268Combined sources7
    Beta strandi273 – 283Combined sources11
    Helixi286 – 291Combined sources6
    Helixi293 – 304Combined sources12
    Helixi308 – 310Combined sources3
    Beta strandi312 – 316Combined sources5
    Helixi321 – 331Combined sources11
    Helixi335 – 337Combined sources3
    Helixi344 – 347Combined sources4
    Turni351 – 353Combined sources3
    Helixi354 – 369Combined sources16
    Beta strandi373 – 380Combined sources8
    Turni381 – 383Combined sources3
    Beta strandi384 – 391Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4O99X-ray1.96A/B/C/D2-393[»]
    4O9AX-ray1.52A/B/C/D2-393[»]
    4O9CX-ray2.00A/B/C/D/E/F/G/H1-393[»]
    ProteinModelPortaliP14611
    SMRiP14611
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CHU Bacteria
    COG0183 LUCA
    HOGENOMiHOG000012238
    KOiK00626
    OMAiICPSIAI

    Family and domain databases

    CDDicd00751 thiolase, 1 hit
    Gene3Di3.40.47.10, 4 hits
    InterProiView protein in InterPro
    IPR002155 Thiolase
    IPR016039 Thiolase-like
    IPR020615 Thiolase_acyl_enz_int_AS
    IPR020610 Thiolase_AS
    IPR020617 Thiolase_C
    IPR020613 Thiolase_CS
    IPR020616 Thiolase_N
    PfamiView protein in Pfam
    PF02803 Thiolase_C, 1 hit
    PF00108 Thiolase_N, 1 hit
    PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
    SUPFAMiSSF53901 SSF53901, 2 hits
    TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
    PROSITEiView protein in PROSITE
    PS00098 THIOLASE_1, 1 hit
    PS00737 THIOLASE_2, 1 hit
    PS00099 THIOLASE_3, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P14611-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTDVVIVSAA RTAVGKFGGS LAKIPAPELG AVVIKAALER AGVKPEQVSE
    60 70 80 90 100
    VIMGQVLTAG SGQNPARQAA IKAGLPAMVP AMTINKVCGS GLKAVMLAAN
    110 120 130 140 150
    AIMAGDAEIV VAGGQENMSA APHVLPGSRD GFRMGDAKLV DTMIVDGLWD
    160 170 180 190 200
    VYNQYHMGIT AENVAKEYGI TREAQDEFAV GSQNKAEAAQ KAGKFDEEIV
    210 220 230 240 250
    PVLIPQRKGD PVAFKTDEFV RQGATLDSMS GLKPAFDKAG TVTAANASGL
    260 270 280 290 300
    NDGAAAVVVM SAAKAKELGL TPLATIKSYA NAGVDPKVMG MGPVPASKRA
    310 320 330 340 350
    LSRAEWTPQD LDLMEINEAF AAQALAVHQQ MGWDTSKVNV NGGAIAIGHP
    360 370 380 390
    IGASGCRILV TLLHEMKRRD AKKGLASLCI GGGMGVALAV ERK
    Length:393
    Mass (Da):40,549
    Last modified:April 1, 1990 - v1
    Checksum:i232C1127E20B3961
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04987 Genomic DNA Translation: AAA21972.1
    AM260479 Genomic DNA Translation: CAJ92573.1
    J05003 Genomic DNA Translation: AAA21976.1
    PIRiA34340 XXALAE
    RefSeqiWP_010810132.1, NC_008313.1

    Genome annotation databases

    EnsemblBacteriaiCAJ92573; CAJ92573; H16_A1438
    KEGGireh:H16_A1438

    Similar proteinsi

    Entry informationi

    Entry nameiTHIL_CUPNH
    AccessioniPrimary (citable) accession number: P14611
    Secondary accession number(s): Q0KBP8
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: March 28, 2018
    This is version 123 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

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