ID A0A1V1ZGG8_9FLAO Unreviewed; 396 AA.
AC A0A1V1ZGG8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OMP31219.1};
GN ORFNames=BKM32_09180 {ECO:0000313|EMBL:OMP31219.1};
OS Mangrovimonas sp. DI 80.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mangrovimonas.
OX NCBI_TaxID=1779330 {ECO:0000313|EMBL:OMP31219.1, ECO:0000313|Proteomes:UP000188854};
RN [1] {ECO:0000313|EMBL:OMP31219.1, ECO:0000313|Proteomes:UP000188854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DI 80 {ECO:0000313|EMBL:OMP31219.1,
RC ECO:0000313|Proteomes:UP000188854};
RA Krishnamurthi S., Pal Y., Verma A., Sundharam S.;
RT "Taxonomic characterization of strain DI 80 closely related to
RT Mangrovimonas sp.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:OMP31219.1}.
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DR EMBL; MSDT01000004; OMP31219.1; -; Genomic_DNA.
DR RefSeq; WP_076663538.1; NZ_MSDT01000004.1.
DR AlphaFoldDB; A0A1V1ZGG8; -.
DR Proteomes; UP000188854; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IPR020615; Thiolase_acyl_enz_int_AS.
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:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000188854};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OMP31219.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
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 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 396 AA; 42699 MW; 626268A4A018C515 CRC64;
MKTAYIVKGY RTAVGKAPKG VFRFKRPDEL AAETIQYMMD QLPEFDKTRI DDVIVGNAMP
EAEQGLNMGR LISLMGLKIE DVPGVTVNRY CASGIETIGI ATAKIQAGMA DCIIAGGAES
MSYIPMGGYK PVPDYAAAKA GHEDYYWGMG LTAEAVAKQF KVSRTDQDEF AFNSHMKALK
AQAEDRFQDQ IVPINVEQVY IDENGKKASK TYTVTKDEGP RKDTNLDALS RLRPVFAADG
SVTAGNSSQM SDGAAFVMVM SEDLVKELNL EPIARLVNYA AAGVEPRIMG IGPVKAIPKA
LKQAGLKQED LSLIELNEAF ASQSIAVIRE LELNPSIVNV NGGAIALGHP LGCTGAKLSV
QLFDEMRKRD MKGKYGAVTM CVGTGQGACG IFEFLN
//
