ID A0A0B4D210_9RHOB Unreviewed; 398 AA.
AC A0A0B4D210;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KIC48813.1};
GN ORFNames=RA29_14135 {ECO:0000313|EMBL:KIC48813.1};
OS Tateyamaria sp. ANG-S1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tateyamaria.
OX NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC48813.1, ECO:0000313|Proteomes:UP000031171};
RN [1] {ECO:0000313|Proteomes:UP000031171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171};
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:KIC48813.1}.
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DR EMBL; JWLL01000006; KIC48813.1; -; Genomic_DNA.
DR RefSeq; WP_039686943.1; NZ_JWLL01000006.1.
DR AlphaFoldDB; A0A0B4D210; -.
DR STRING; 1577905.RA29_14135; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000031171; 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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000031171};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KIC48813.1}.
FT DOMAIN 5..267
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 276..396
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 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 398 AA; 41824 MW; C004AF33B24218B2 CRC64;
MRDAVIVSTA RTPIGKAYRG AFNATPPQTL AAHAIEHAVK RAGLNGAEVQ DVIMGAALQQ
GHQAGNVARQ AAIRAGLPVT VAGMSVDRQC ASGMMAIATA SKQVVHDGME VVVGGGVESV
SMVQTQEMRT HADPWLKQNK PEIYMTMLET AETVAARYGV SREAQDRYAV QSQARTAAAQ
EAGKFDDEIV PLSTVMKFQD KETKAISEHE VTLDKDEGNR PETTYENVAG LKPVFANGIH
VEQGEYITAG NASQLSDGAS AAVVMEASLA EKKGLSPLGR CVGVMAAGCE PDEMGIGPVF
AVPKLLEAHG LGMDDIGLWE LNEAFAVQVL YCRDTLGIPD ELLNVNGGAI SIGHPYGMSG
ARMVGHALIE GKRRGAKHVV CTMCVGGGMG AAGLFEVL
//
