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Database: UniProt
Entry: K2KAL7_9GAMM
LinkDB: K2KAL7_9GAMM
Original site: K2KAL7_9GAMM 
ID   K2KAL7_9GAMM            Unreviewed;       393 AA.
AC   K2KAL7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EKE84883.1};
GN   ORFNames=A10D4_04705 {ECO:0000313|EMBL:EKE84883.1};
OS   Idiomarina xiamenensis 10-D-4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=740709 {ECO:0000313|EMBL:EKE84883.1, ECO:0000313|Proteomes:UP000014115};
RN   [1] {ECO:0000313|EMBL:EKE84883.1, ECO:0000313|Proteomes:UP000014115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10-D-4 {ECO:0000313|EMBL:EKE84883.1,
RC   ECO:0000313|Proteomes:UP000014115};
RX   PubMed=23209204; DOI=10.1128/JB.01855-12;
RA   Lai Q., Wang L., Wang W., Shao Z.;
RT   "Genome Sequence of Idiomarina xiamenensis Type Strain 10-D-4.";
RL   J. Bacteriol. 194:6938-6938(2012).
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:EKE84883.1}.
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DR   EMBL; AMRG01000004; EKE84883.1; -; Genomic_DNA.
DR   RefSeq; WP_008488052.1; NZ_AMRG01000004.1.
DR   AlphaFoldDB; K2KAL7; -.
DR   STRING; 740709.A10D4_04705; -.
DR   PATRIC; fig|740709.3.peg.954; -.
DR   eggNOG; COG0183; Bacteria.
DR   OrthoDB; 8951704at2; -.
DR   Proteomes; UP000014115; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR18919:SF144; ACYL-COA THIOLASE-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.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014115};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EKE84883.1}.
FT   DOMAIN          6..262
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          270..391
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        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   393 AA;  40856 MW;  BE465C387A4D1E93 CRC64;
     MSDQAIVIVA AKRTPMGGFQ GSLSSLPAPE LGAAAIKAAL DSAKLDAASV SEVIMGNVLP
     AGLGQAPARQ AMLKAGLARA TGATTINKVC GSGLKAVMLA HDLIKAGSAE VVVAGGMESM
     SNAPYMLPKA RNGYRMGHGQ VLDHMMLDGL EDAYEHKAMG CFAQVTADEY QLGREAMDEF
     AINSLKKAQQ AIGDGHFSQE ITPLTLTTRQ GEVTVDTDEQ PGKAKLDKIP QLRAAFAKDG
     TITAANSSSI SDGAAALVLM TEAQAKALGL QPLARIVGHS THSQAPAEFT VAPIGAMTSL
     LQRIGWDKEQ VDLWEINEAF AMVTMLAIEE MQLDADKVNV HGGACALGHP IGASGARLLV
     TLLHALKQRG KQRGITSLCI GGGEAVALAV EML
//
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