ID A0A2S4HAW9_9GAMM Unreviewed; 400 AA.
AC A0A2S4HAW9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acetyl-CoA C-acyltransferase {ECO:0000313|EMBL:POP51123.1};
GN ORFNames=C0068_19275 {ECO:0000313|EMBL:POP51123.1};
OS Marortus luteolus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Marortus.
OX NCBI_TaxID=2067667 {ECO:0000313|EMBL:POP51123.1, ECO:0000313|Proteomes:UP000237222};
RN [1] {ECO:0000313|EMBL:POP51123.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZX-21 {ECO:0000313|EMBL:POP51123.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:POP51123.1}.
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DR EMBL; PQGG01000044; POP51123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4HAW9; -.
DR OrthoDB; 8951704at2; -.
DR Proteomes; UP000237222; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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; 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.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:POP51123.1}.
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; 42250 MW; 2D1D0FDFEE6BA6B5 CRC64;
MKEAVIVSTA RTGMGKSFRG ALNNTEAPAM GGHVVRAAVE RAGIDPASVE DVIFGAAAQQ
GTQAYNLGRL CAVAGGLPDS VPGMAIERQC SSGLMSIAWA AKSIMCNEID IAVAGGLESI
SLVQTKHKNS YRNVSQTVLD IDPTAYIPMI ETAEIVSDRY GISREAQDIY SLQSQQRVAA
AQQAGLFSAE IVPFATSMSV FNKDTKETTF KDVILESDEC NRPSTSLESL ASLEPVFKDG
QWVKQGRFIT AGNASQLSDG ASACVVMDRK LAEQKGLSPL GIYRGMAVAG CKADEMGIGP
VFAIPKLLKR AGLKVDDIGL WELNEAFACQ VIYCRDQLGI DNDKLNVNGG SIAIGHPFGM
SGARMVGHAL IEGKRRGVKY AVVTMCIGGG MGAAALFEIA
//
