ID A0A2A2F5N4_9GAMM Unreviewed; 445 AA.
AC A0A2A2F5N4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Acetyl-CoA C-acyltransferase {ECO:0000313|EMBL:PAU80756.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:PAU80756.1};
GN ORFNames=CK501_10130 {ECO:0000313|EMBL:PAU80756.1};
OS Halovibrio salipaludis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halovibrio.
OX NCBI_TaxID=2032626 {ECO:0000313|EMBL:PAU80756.1, ECO:0000313|Proteomes:UP000218896};
RN [1] {ECO:0000313|EMBL:PAU80756.1, ECO:0000313|Proteomes:UP000218896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL5-2 {ECO:0000313|EMBL:PAU80756.1,
RC ECO:0000313|Proteomes:UP000218896};
RA Dong X., Zhang G.;
RT "Halovibrio sewagensis sp. nov., isolated from wastewater of high
RT salinity.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {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:PAU80756.1}.
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DR EMBL; NSKD01000003; PAU80756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2F5N4; -.
DR OrthoDB; 8951704at2; -.
DR Proteomes; UP000218896; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:PAU80756.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218896};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:PAU80756.1}.
FT DOMAIN 27..294
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 303..444
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 401
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 431
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 445 AA; 47436 MW; A357C78554F91D49 CRC64;
MAQAKSTSSK SRQSKGNGAA ATLPRPVAIL GGNRIPFARS NTAYSKLSNQ DMLTAAIRGL
VDRYGLEGER LGEVVAGAVI KHSRDFNLTR ETVLGSGLAP ETPAYDIQQA CGTGLEAAIL
VANKIALGQV DAGIAGGTDT TSDAPIGVSE GLRELLLDLN RAKTNTERLK IAARFRPKHL
VPLIPENSEP RTGMSMGEHQ QVTAHEWGIP REEQDQLALE SHQKLAAAYE EGFFSDLITP
LAGLERDNIL RPDSSLEKLS QLKPVFDKEK GTMTAANSTA LTDGASSVLL GSEEWAQQRG
LKVRAYLTHV ETGAVDFVGK KEGLLMAPAY AVPRLLDKAG LTLQDFDFYE IHEAFASQVL
CTLRAWEDQT FCKEKLGLSK PLGSIDRDRL NVKGSSLAAG HPFAATGARI LATAAKLLEQ
KGSGRALISI CAAGGQGVTA IVERG
//
