ID M4S755_9SPHN Unreviewed; 398 AA.
AC M4S755;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AGH51855.1};
GN ORFNames=G432_20865 {ECO:0000313|EMBL:AGH51855.1};
OS Sphingomonas sp. MM-1.
OG Plasmid pISP1 {ECO:0000313|EMBL:AGH51855.1,
OG ECO:0000313|Proteomes:UP000011816}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH51855.1, ECO:0000313|Proteomes:UP000011816};
RN [1] {ECO:0000313|EMBL:AGH51855.1, ECO:0000313|Proteomes:UP000011816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM-1 {ECO:0000313|EMBL:AGH51855.1};
RC PLASMID=Plasmid pISP1 {ECO:0000313|Proteomes:UP000011816};
RX PubMed=23682148;
RA Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT Bacterium Sphingomonas sp. Strain MM-1.";
RL Genome Announc. 1:E00247-13(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; CP004038; AGH51855.1; -; Genomic_DNA.
DR AlphaFoldDB; M4S755; -.
DR KEGG; sphm:G432_20865; -.
DR PATRIC; fig|745310.14.peg.4333; -.
DR HOGENOM; CLU_031026_0_0_5; -.
DR Proteomes; UP000011816; Plasmid pISP1.
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; -; 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; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Plasmid {ECO:0000313|EMBL:AGH51855.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011816};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AGH51855.1}.
FT DOMAIN 4..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..392
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
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 398 AA; 41147 MW; 76DF2C401997A1E5 CRC64;
MNDVVILSGV RTAIGDFGGS LKDVAPWELG RVVIAEAIKR AGIEPGDVEH VVLGQVIQSE
PRDAYVSRIA AIAAGIPDRT PALTLNRLCG SSVQAIVSAA QMIALGECSI AVAGGVESMS
QSPHVLKGLR WGRRMGDEMM IDAMNATLSD PFGAGHMGVT AENVAERHGI TRAEQDALAA
ESHRRAARAQ QEGRFREQIV PVEIKGRGGA HMFEVDEHVR ADVSSEALGV LQPIFRKDGG
TVTAGNASGI NDAGAALVLA SAATAETCGL TPRARVVSWG HAGVAPEVMG LGPVEAVPIA
LKRAGLSLDD IDVIEANEAF AAQACAVAKL LDLPPEKVNP NGSGIGLGHP VGATGAIITI
KALYELERIG GRYGLVTMCI GGGQGIALVI ERWPAGEA
//
