ID A0A1S3FUD0_DIPOR Unreviewed; 321 AA.
AC A0A1S3FUD0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-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 Name=LOC105991805 {ECO:0000313|RefSeq:XP_012879985.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012879985.1};
RN [1] {ECO:0000313|RefSeq:XP_012879985.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012879985.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR RefSeq; XP_012879985.1; XM_013024531.1.
DR AlphaFoldDB; A0A1S3FUD0; -.
DR GeneID; 105991805; -.
DR KEGG; dord:105991805; -.
DR InParanoid; A0A1S3FUD0; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000081671; Unplaced.
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; -; 3.
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; PTHR18919:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 2.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 8..70
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 81..191
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 198..320
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 321 AA; 33541 MW; AAA564988673D728 CRC64;
MNAGSDPVVI VAAARTVIGS FNGALSTVPA HDLGATVIKE VLKRAAVAPE EVSEVIFGHV
LAAGKGSILA SWWMWGLSEN CQSMGITAEN VAKQWQVSRE DQDKVALLSQ NRTEHAQKAG
HFDKEIVPVL VSSRKGITEV KTDEFPRHGS NLEALAKLKP YFLTDGTGTV TAANASGIND
GAAAVVLMKK SEAENRGLKP LAQIVSWSQA GVDPSIMGTG PIPAIKQAVF KAGWSLEDVD
AFEINEAFAA VSAAIAKELG LCPEKVNIEG GAIALGHPLG ASGCRILVTL LHTLERMDKS
RGVAALCIGG GMGIAMCVQR G
//
