ID K4KIN9_SIMAS Unreviewed; 394 AA.
AC K4KIN9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AFU98891.1};
GN OrderedLocusNames=M5M_08510 {ECO:0000313|EMBL:AFU98891.1};
OS Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Simiduia.
OX NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFU98891.1, ECO:0000313|Proteomes:UP000000466};
RN [1] {ECO:0000313|EMBL:AFU98891.1, ECO:0000313|Proteomes:UP000000466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC {ECO:0000313|Proteomes:UP000000466};
RX PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT bacterium able to degrade a variety of polysaccharides.";
RL Genome Announc. 1:E00039-E00039(2013).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP003746; AFU98891.1; -; Genomic_DNA.
DR RefSeq; WP_015047056.1; NZ_ATUQ01000002.1.
DR AlphaFoldDB; K4KIN9; -.
DR STRING; 1117647.M5M_08510; -.
DR KEGG; saga:M5M_08510; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_1_1_6; -.
DR OrthoDB; 8951704at2; -.
DR Proteomes; UP000000466; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000466};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AFU98891.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..391
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 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 41138 MW; D1546DDB54FBCF6C CRC64;
MKEAVIVSVA RTPIGKAYRG AFNNLTSPSL SAVAVQAAVE RAGIAPEEID DCVWGAALQQ
GSQGTNLGRQ VAMAAGLPVS VAGMTLDRQC ASGLMAVATA AKQIVLDHVP VVLAGGTESI
SLVQNQHMNS HRTEDALVLQ HTPDLYMPML DTAEVVAKRY NISRAAQDEY AVMSQARTAE
AQAAGKFADE IVPVNATKLV QDKTTGAVSE QAVSLTQDEG NRPGTTIESL ASLNAVREGG
SITAGNASQL SDGAAALVLM DRTLAEERGL KPLGVYRGMA VAGCAPDEMG IGPVFAVPKL
LQRAGLTMAD IGLWELNEAF AVQVLYCAQR LAIPMDRLNV NGGAISIGHP YGMSGARMVM
HALLEGRRRG VRYVVVTMCV GGGMGAAGLF EVLQ
//
