ID A0A0C1GCY4_9RHOB Unreviewed; 391 AA.
AC A0A0C1GCY4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KIC40071.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KIC40071.1};
GN ORFNames=RA27_14610 {ECO:0000313|EMBL:KIC40071.1};
OS Ruegeria sp. ANG-R.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577903 {ECO:0000313|EMBL:KIC40071.1, ECO:0000313|Proteomes:UP000031318};
RN [1] {ECO:0000313|Proteomes:UP000031318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-R {ECO:0000313|Proteomes:UP000031318};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC40071.1}.
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DR EMBL; JWLJ01000006; KIC40071.1; -; Genomic_DNA.
DR RefSeq; WP_039540509.1; NZ_JWLJ01000006.1.
DR AlphaFoldDB; A0A0C1GCY4; -.
DR STRING; 1577903.RA27_14610; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000031318; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KIC40071.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KIC40071.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 40732 MW; 5B7BEBFF945DD6E7 CRC64;
MTNVVIASAA RTGVGSFSGS FANTPAHDLG AAVLEAVVER AGIDKGEVSE TIMGQVLTAA
QGQNPARQAH INAGLPQESA AWGINQVCGS GLRAVALGAQ HIQLGDAEIV AAGGQENMTL
SPHAAALRAG HKMGDMKYID TMIRDGLWDA FNGYHMGQTA ENVAEKWQIS RDMQDEFAVA
SQNKAEAAQN AGKFADEIVP FTIKTRKGDI VMDKDEYIRH GATIEAMGKL RPAFAKDGSV
TAANASGLND GAAATLLMSA ENAEKRGIEP LARIASYATA GLDPSIMGVG PIYASRKALE
KAGWSVDDLD LVEANEAFAA QACAVNKDMG WDPSIVNVNG GAIAIGHPIG ASGCRVLNTL
LFEMKRRDAK KGLATLCIGG GMGVALCVER D
//
