ID A0A423PIG1_9GAMM Unreviewed; 400 AA.
AC A0A423PIG1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ROO25429.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ROO25429.1};
GN ORFNames=SAOR_12845 {ECO:0000313|EMBL:ROO25429.1};
OS Salinisphaera orenii MK-B5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=856730 {ECO:0000313|EMBL:ROO25429.1, ECO:0000313|Proteomes:UP000283993};
RN [1] {ECO:0000313|EMBL:ROO25429.1, ECO:0000313|Proteomes:UP000283993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK-B5 {ECO:0000313|EMBL:ROO25429.1,
RC ECO:0000313|Proteomes:UP000283993};
RA Lai Q., Li C., Shao Z.;
RT "Salinisphaera orenii MK-B5 Genome Sequencing.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:ROO25429.1}.
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DR EMBL; AYKH01000034; ROO25429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423PIG1; -.
DR Proteomes; UP000283993; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF22; ACETYL-COA ACETYLTRANSFERASE; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000283993};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ROO25429.1}.
FT DOMAIN 5..269
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..398
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 356
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 400 AA; 43013 MW; 394422FBD2A9B32A CRC64;
MRQAVIVSTA RTPIGKAYRG AFNDTQAQAL GGHAIEHALK RAKLEGENID DVIMGAALQQ
GATGQNVARQ CALRAGLPTS VPGMTIDRQC ASGLMGIATA AKQIVNDRMD VIVGGGLESI
SLVQNEHYNR HRARDPWLVD HRPDIYMSML ETAEVVADRY NVSREAQDEY AYQSQMRTAA
AQEAGRFDDE IVPLTTVKKV MDKETGEVHD EEVTLDKDEG NRPSTTLEGL QQLKPVFKDG
MEVAEGRFIT AGNASQLSDG ASASVLMEAA EAERRGLEPL GAYVGMAVAG CDPDEMGIGP
IYAVPKLLER YGLKVDDIGL WELNEAFASQ CLYCRDFLGI DPDLYNVDGG SIAIGHPYGM
SGARMTGHAL IEGKRRGAKY VVVTMCVGGG IGAAGLFEVF
//
