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Database: UniProt
Entry: A0A0P7VBU0_SCLFO
LinkDB: A0A0P7VBU0_SCLFO
Original site: A0A0P7VBU0_SCLFO 
ID   A0A0P7VBU0_SCLFO        Unreviewed;       342 AA.
AC   A0A0P7VBU0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN   ORFNames=Z043_100464 {ECO:0000313|EMBL:KPP79917.1};
OS   Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX   NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP79917.1, ECO:0000313|Proteomes:UP000034805};
RN   [1] {ECO:0000313|EMBL:KPP79917.1, ECO:0000313|Proteomes:UP000034805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aro1 {ECO:0000313|EMBL:KPP79917.1};
RA   Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT   "The genome of the Asian arowana (Scleropages formosus).";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + propanoyl-CoA = 2-methyl-3-oxobutanoyl-CoA + CoA;
CC         Xref=Rhea:RHEA:30719, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57335, ChEBI:CHEBI:57392;
CC         Evidence={ECO:0000256|ARBA:ARBA00036841};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30720;
CC         Evidence={ECO:0000256|ARBA:ARBA00036841};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30721;
CC         Evidence={ECO:0000256|ARBA:ARBA00036841};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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:KPP79917.1}.
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DR   EMBL; JARO02000100; KPP79917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7VBU0; -.
DR   STRING; 113540.ENSSFOP00015071689; -.
DR   Proteomes; UP000034805; Unassembled WGS sequence.
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; -; 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; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919:SF156; ACETYL-COA ACETYLTRANSFERASE, MITOCHONDRIAL; 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; 2.
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|RuleBase:RU003557};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034805};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          5..107
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          222..341
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        89
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        300
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        328
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   BINDING         134
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-2"
FT   BINDING         173..175
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-2"
FT   BINDING         178
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-2"
FT   BINDING         199
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-2"
SQ   SEQUENCE   342 AA;  35600 MW;  6CBD8695FFFB7CC8 CRC64;
     MSVEVVIVSA VRTPVGSFMG SLSTVPATQL GSIAIKGAVE RAGIPVEEVK EVYMGNVLQA
     GEGQAPTRQA LLGAGLPIST PATTVNKVCA SGMKSVMLAA QSLMCGHQGN CAENTAKNSG
     ISREEQDKYA ISSYTRSKAA WESGVLAKEV VPVSIPQRGK PDLVVSEDEE FRRVDFSKVP
     KLKAVFQKEN GTVTAANAST LNDGAAALVL MTTDAAKRLN ATPLARIVCF ADAAVAPIDF
     PIAPAFAVPK ILKTSGVKKE DIAMWEINEA FSVVVLANIK MLDIDPSKVN MNGGAVSLGH
     PIGMSGARIV GHMVHNLKPG QYGLAGICNG GGGASSILIQ RF
//
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