ID A0A254QJD8_9RHOB Unreviewed; 394 AA.
AC A0A254QJD8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OWU69830.1};
GN ORFNames=ATO1_24420 {ECO:0000313|EMBL:OWU69830.1};
OS Phaeobacter sp. 22II1-1F12B.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1317111 {ECO:0000313|EMBL:OWU69830.1, ECO:0000313|Proteomes:UP000197279};
RN [1] {ECO:0000313|EMBL:OWU69830.1, ECO:0000313|Proteomes:UP000197279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II1-1F12B {ECO:0000313|EMBL:OWU69830.1,
RC ECO:0000313|Proteomes:UP000197279};
RA Lai Q., Li G., Shao Z.;
RT "Phaeobacter sp. 22II1-1F12B Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:OWU69830.1}.
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DR EMBL; AQQP01000035; OWU69830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254QJD8; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000197279; 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:UP000197279};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OWU69830.1}.
FT DOMAIN 5..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..392
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 204..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 40637 MW; B5D6BA98AA728590 CRC64;
MKDAAILSTA RTGIGRAFKG ALNNTKSPTL MGHAMRHALD RAGVDGAEVD DVVIGTVLAS
GTAGMNIARN AAFAAGLPVT VAAQTMDRQC ASGLMAVATA AKQIMVDGMT ITMAGGQDNI
SAVQGPYFDS VMTSIDPNVT ARVPHAYMPM LKTAEFVADK YGISREAQDT YALSSQQRTA
AAQASGRFDA EVVPFSTTML VKDKASGETS EVPVTLEGDE GNRPDTTAES LAGLKPVIEG
GSVTAGNASQ LSDGASALVM MEGAEAERRG LSPLGFYRGI AVAGCAPEEM GIGPVYAVPK
LLRQHGLGVG DIGLWELNEA FACQAIYCRD TLGIDPEIYN VNGGGISIGH PYGMTGARLV
GHALIEGKRR GVRYVVVTMC VGGGMGAAGL FEVA
//
