ID A3VK33_9RHOB Unreviewed; 367 AA.
AC A3VK33;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EAQ11338.1};
GN ORFNames=RB2654_23288 {ECO:0000313|EMBL:EAQ11338.1};
OS Maritimibacter alkaliphilus HTCC2654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ11338.1, ECO:0000313|Proteomes:UP000002931};
RN [1] {ECO:0000313|EMBL:EAQ11338.1, ECO:0000313|Proteomes:UP000002931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ11338.1,
RC ECO:0000313|Proteomes:UP000002931};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
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:EAQ11338.1}.
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DR EMBL; AAMT01000016; EAQ11338.1; -; Genomic_DNA.
DR RefSeq; WP_008327527.1; NZ_VNHV01000010.1.
DR AlphaFoldDB; A3VK33; -.
DR STRING; 314271.RB2654_23288; -.
DR HOGENOM; CLU_031026_2_1_5; -.
DR OrthoDB; 7838428at2; -.
DR Proteomes; UP000002931; 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; -; 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; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000002931};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EAQ11338.1}.
FT DOMAIN 4..237
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 256..364
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 120..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 37236 MW; 04AD7F49420CFB56 CRC64;
MSGVRVVSAL RTPVAPRGGG LARLDLDALC APVLAKAIRE AGLGVEDVDE VVLGNALGAG
GNPARRVALA AGLPERVAGL TLDRQCCGGL DALVMGAALI ASGQAEVVAA GGVESYSRRP
LRLRTDPDGG PPVAYDRPPF TPWPDRDPEM DEAAEALARS WNIARAAQDA WAVDSHRKAR
MAEMRGEVVP LAGVERDTFT RDLTPRLAAR APGLVGSITA ANAAVAADGA AVCLLVSDRV
AARLPDPGLA YRGGITLGAR PDLPGVAPVE AIRALFDRTG TTPADLSVAE VMEAYAVQAI
ACVEGAGLDP AIVNPGGGGL ARGHPVGASG AINAVRLWHE VKRRGGTGLA AIAAAGGLGT
AVMLSVR
//
