THIL_SYNY3
ID THIL_SYNY3 Reviewed; 396 AA.
AC P73825;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000255|PROSITE-ProRule:PRU10020};
DE EC=2.3.1.9 {ECO:0000255|PROSITE-ProRule:PRU10020};
DE AltName: Full=Beta-ketothiolase PhaA {ECO:0000303|PubMed:11010896};
GN Name=phaA {ECO:0000303|PubMed:11010896}; OrderedLocusNames=slr1993;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND EXPRESSION IN E.COLI.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=11010896; DOI=10.1128/aem.66.10.4440-4448.2000;
RA Taroncher-Oldenburg G., Nishina K., Stephanopoulos G.;
RT "Identification and analysis of the polyhydroxyalkanoate-specific beta-
RT ketothiolase and acetoacetyl coenzyme A reductase genes in the
RT cyanobacterium Synechocystis sp. strain PCC6803.";
RL Appl. Environ. Microbiol. 66:4440-4448(2000).
CC -!- FUNCTION: When expressed in E.coli with Synechocystis PhaB, PhaC and
CC PhaE confers the ability to synthesize up to 12% (w/w) poly(3-
CC hydroxybutyrate) (PHB) depending on the carbon source.
CC {ECO:0000269|PubMed:11010896}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
CC -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC biosynthesis. {ECO:0000269|PubMed:11010896}.
CC -!- SUBUNIT: Homotetramer (By similarity). {ECO:0000250|UniProtKB:P14611}.
CC -!- DISRUPTION PHENOTYPE: Double deletion of phaA and phaB leads to loss of
CC synthesis of PHB, no visible growth phenotype.
CC {ECO:0000269|PubMed:11010896}.
CC -!- BIOTECHNOLOGY: Poly(3-hydroxyalkanoic acids) (PHA), of which PHB is
CC among the most common compounds, are prokaryotic intracellular storage
CC compounds with potential uses as renewable, biodegradable
CC thermoplastics. Cyanobacterial PHB synthesis is particularly attractive
CC as cyanobacteria use CO(2) as the carbon source. {ECO:0000305}.
CC -!- MISCELLANEOUS: Nitrogen-free medium induces chlorosis in Synechocystis,
CC leading to the degradation of the photosynthetic apparatus and
CC concomitant accumulation of cytoplasmic polyhydroxyalkanoic acid (PHA)
CC granules which in this cyanobacterium are composed of PHB.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA17882.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000022; BAA17882.1; ALT_INIT; Genomic_DNA.
DR PIR; S75020; S75020.
DR AlphaFoldDB; P73825; -.
DR SMR; P73825; -.
DR IntAct; P73825; 1.
DR STRING; 1148.1652965; -.
DR PaxDb; P73825; -.
DR EnsemblBacteria; BAA17882; BAA17882; BAA17882.
DR KEGG; syn:slr1993; -.
DR eggNOG; COG0183; Bacteria.
DR InParanoid; P73825; -.
DR PhylomeDB; P73825; -.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase; PHB biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000438830"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P14611"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14611"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14611"
SQ SEQUENCE 396 AA; 41710 MW; 418BC995D54F8776 CRC64;
MRDVFIVAAK RTPLGRFGGS LTNFSAADLG AHVMKSVLAQ AGVGGDQLDL YIMGNVLRAG
HGQLIPRQAA LKAEIPDTVD GYAVDMVCSS AMMSVINAAL TIRAGEGDLI LAGGTESMSQ
TGFYLSHRAR WGYKFLMGAP ENLTDLLLHD GLTDSTNGEG MGEQTEKLAA EHGFSRIELD
EVACLSQQRA AHATESGYFD SEIAPIEITS RKGTQVLASD EGIRSDTTVE SLGKLRSAFA
KDGVLTAGNC SQITDGAAAL LLASGEAVEK YQLKPLAKIL GGSWAAGTPS RFPELPITAS
QKLLAKLDKT LADFDLFENN EAFSVSNLLF ERRLGVDRDK LNVNGGAIAL GHPIGASGAR
IMVTLLYALQ QRDKTLGLAA LCHGTGGGTA IALERV
