ID A7HQA4_PARL1 Unreviewed; 401 AA.
AC A7HQA4;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ABS62087.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:ABS62087.1};
GN OrderedLocusNames=Plav_0464 {ECO:0000313|EMBL:ABS62087.1};
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS62087.1, ECO:0000313|Proteomes:UP000006377};
RN [1] {ECO:0000313|EMBL:ABS62087.1, ECO:0000313|Proteomes:UP000006377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966
RC {ECO:0000313|Proteomes:UP000006377};
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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; CP000774; ABS62087.1; -; Genomic_DNA.
DR RefSeq; WP_011995378.1; NC_009719.1.
DR AlphaFoldDB; A7HQA4; -.
DR STRING; 402881.Plav_0464; -.
DR KEGG; pla:Plav_0464; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_3_5; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000006377; Chromosome.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
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; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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 ECO:0000313|EMBL:ABS62087.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006377};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABS62087.1}.
FT DOMAIN 5..228
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..400
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 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 401 AA; 42252 MW; 3E41BD754B3BF2C1 CRC64;
MTECFVYDAV RTPRGKGKKD GALHEVTALE LSTQTLKAIR DRNDLDTSKV DDVVLGCVDP
VGEQGGDIAR IAVLNADYAQ TTAGVQINRF CASGLEATNM AAAKVMSGEA DMAIGGGVES
MSRVGMGASG GSWSTDPNIA FKSYFTPQGI GADLISTKYG FSRADVDAYA VESQKRAKNA
WDKGYFSKSV IPVKDINGLT ILDHDEHMRP DATMQSLAAL QPSFASLGEF AFDGVALDRY
PEIEEINHMH HAGNSSGIVD GASAVLVGNG PTGKALGLKP RARIRAMASI GSEPCIMLTG
PADVSRKALA KAGMKPEDID LYELNEAFAS VVLRMMQALD IPHDKMNVNG GAIAMGHPLG
ATGGMILGTV LDELERRDLN TALITLCVGA GMGTATIIER V
//
