ID A0A438AEH2_9RHOB Unreviewed; 392 AA.
AC A0A438AEH2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:RVV97077.1};
GN ORFNames=EKE94_15565 {ECO:0000313|EMBL:RVV97077.1};
OS Mesobaculum littorinae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Mesobaculum.
OX NCBI_TaxID=2486419 {ECO:0000313|EMBL:RVV97077.1, ECO:0000313|Proteomes:UP000285908};
RN [1] {ECO:0000313|EMBL:RVV97077.1, ECO:0000313|Proteomes:UP000285908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M0103 {ECO:0000313|EMBL:RVV97077.1,
RC ECO:0000313|Proteomes:UP000285908};
RA Li F.;
RT "Mesobaculum littorinae gen. nov., sp. nov., isolated from Littorina scabra
RT that represents a novel genus of the order Rhodobacteraceae.";
RL Submitted (NOV-2018) 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:RVV97077.1}.
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DR EMBL; RQXX01000006; RVV97077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A438AEH2; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000285908; 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; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_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; 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.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000285908};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RVV97077.1}.
FT DOMAIN 6..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..391
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 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 392 AA; 40950 MW; 6684E0A981B79D0A CRC64;
MTEAAYIVAA RRAPIGRLCG AYTGIAAARL GAQVMRAVIE DAGIDPGIID EVIAGQVLQG
GAGQNPARQA AIHAGIPDHV PAMTINKVCG AGQKSIHLAA QAIRAGDAHV ILATGQDSMT
EAPHLLPGVR TGRKMGDMTA KDMMIVDGLW DVFNDVHMGT TVESLARRYQ ITREEQDAFA
LASQEKALAA QSAGIFETEI TPITIQDRKG DRTVERDEQP RETTMERLAG MTPAFDRAGT
ITPGNASGLN DGASAVLVVS ESKLRELGLT PMARIASYAA AALEPMDMGL GPVEASRKAL
EKAGWTAKDL DRMEINEAFA AQSLAVNREM GWDPSAINVN GGAIALGHPL AASGNRIVTT
LLHEMARSGS GKGLASLCIG GGMGVAICLE RA
//
