ID A0A077LGA4_9PSED Unreviewed; 392 AA.
AC A0A077LGA4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:BAP41968.1};
GN ORFNames=PSCI_1266 {ECO:0000313|EMBL:BAP41968.1};
OS Pseudomonas sp. StFLB209.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP41968.1, ECO:0000313|Proteomes:UP000031652};
RN [1] {ECO:0000313|EMBL:BAP41968.1, ECO:0000313|Proteomes:UP000031652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StFLB209 {ECO:0000313|EMBL:BAP41968.1,
RC ECO:0000313|Proteomes:UP000031652};
RX PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA Morohoshi T., Kato T., Someya N., Ikeda T.;
RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL Genome Announc. 2:e01037-e01014(2014).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; AP014637; BAP41968.1; -; Genomic_DNA.
DR RefSeq; WP_045484346.1; NZ_AP014637.1.
DR AlphaFoldDB; A0A077LGA4; -.
DR STRING; 1028989.PSCI_1266; -.
DR KEGG; pses:PSCI_1266; -.
DR HOGENOM; CLU_031026_0_0_6; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000031652; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000031652};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:BAP41968.1}.
FT DOMAIN 4..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..391
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 392 AA; 40368 MW; 229471F4CAAC6DF4 CRC64;
MQDVVIVAAT RTAIGSFQGA LAGIPAPELG ALVIRRLLEQ TGLDAAQVDE VILGQVLTAG
SGQNPARQAS ILAGLPHSVP ALTLNKVCGS GLKAIHLGAQ AIRCGDAEVI IAGGMENMSL
APYVLPAART GLRMGHAQMV DSMITDGLWD AFNDYHMGIT AENLVAKYGI SREAQDAFAA
ASQHKAIAAI EAGRFKDEIT PVSIPQKKGE PRLFDTDEQP RAETSAESLA KLRPAFRKDG
SVTAGNASSL NDGAAAVLLM SAAKAAELGL PVLASIKAYA NAGVDPAIMG IGPVAATRRC
LDKAGWQLNE LDLIEANEAF AAQALSVGQE LGWDASKVNV NGGAIALGHP IGASGCRVLV
TLLHEMIRRD AKKGLATLCI GGGQGVALAI AR
//
