ID S3E0G1_9GAMM Unreviewed; 408 AA.
AC S3E0G1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Acetyl-coA acetyltransferase {ECO:0000313|EMBL:EPE37676.1};
GN ORFNames=O1U_0132 {ECO:0000313|EMBL:EPE37676.1};
OS Candidatus Photodesmus katoptron Akat1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photodesmus.
OX NCBI_TaxID=1236703 {ECO:0000313|EMBL:EPE37676.1, ECO:0000313|Proteomes:UP000053688};
RN [1] {ECO:0000313|EMBL:EPE37676.1, ECO:0000313|Proteomes:UP000053688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Akat1 {ECO:0000313|EMBL:EPE37676.1,
RC ECO:0000313|Proteomes:UP000053688};
RX PubMed=24118864; DOI=10.1111/1462-2920.12302;
RA Hendry T.A., de Wet J.R., Dunlap P.V.;
RT "Genomic signatures of obligate host dependence in the luminous bacterial
RT symbiont of a vertebrate.";
RL Environ. Microbiol. 16:2611-2622(2014).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPE37676.1}.
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; AMSD01000001; EPE37676.1; -; Genomic_DNA.
DR RefSeq; WP_016503474.1; NZ_AMSD01000001.1.
DR AlphaFoldDB; S3E0G1; -.
DR STRING; 28176.CF66_2296; -.
DR PATRIC; fig|1236703.3.peg.119; -.
DR eggNOG; COG0183; Bacteria.
DR Proteomes; UP000053688; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; -; 1.
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:SF164; ACETYL-COA ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053688};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EPE37676.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 385..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..267
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 275..405
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 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 408 AA; 43138 MW; CAB8872A599CC27B CRC64;
MKKVYAISGK RTPIGAFCGS LKGISAGKLA SIAIEGALAS AKVSPSILDE VIIGNVISAG
QGMGIARQAA IYAGIPKSVP AYGINMVCGS GMKAVMDGVA HIKNNDADIV IAGGVEVMSQ
IPFILPSSIR SGHKQHKMGN LTLIDLLISD GLTDVYTKHH MGMTAETIAK EFSITRKQQD
SYAMTSQFKA VDAIKKGKFV NEIETVNVSQ PRKSNVFFDT DEYPRKEVKL SELEKLAPAF
QKEGTVTAGN SSGLNDGASA MVLASEESIE KYNLSPIAEI ISYAQSALEP EMMGLGPVNS
IKKALNKAQL SISDINLYEL NEAFAVQTLA VIHKLADEYN VSVSSILDKT NVNGGAISLG
HPLGASGNRI LVTLMHELNR NKKKSHFGIA ALCIGGGMGT AVIIKTVT
//
