ID Q2SGR7_HAHCH Unreviewed; 435 AA.
AC Q2SGR7;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ABC30157.1};
GN OrderedLocusNames=HCH_03408 {ECO:0000313|EMBL:ABC30157.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC30157.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC30157.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC30157.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC30157.1; -; Genomic_DNA.
DR RefSeq; WP_011397225.1; NC_007645.1.
DR AlphaFoldDB; Q2SGR7; -.
DR STRING; 349521.HCH_03408; -.
DR KEGG; hch:HCH_03408; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR OrthoDB; 8951704at2; -.
DR Proteomes; UP000000238; Chromosome.
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; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABC30157.1}.
FT DOMAIN 12..286
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 293..431
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 96
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 435 AA; 46528 MW; 42384F074C20976B CRC64;
MSIQESQPSE PVYVVDGARS PFIKAGDRPG PFHAGDLAAQ TGAALLLRQP FNAEEIDEVI
LGNTMAGPEE ANIGRVAALR MGCGEATPGY TVHRNCASGM QALDNAAASI ADGRSDLILA
GGVEAMSHAP VLLREDMLNW LADWRNADSP LEKIKLIPEF ETQYVQPVIG LLRGLTDPIV
GLNMGQTTEK EAEHFGVSRR SMDEYAALSQ QRLAHADGAG YFKEERTSLY SPDGTFFDKD
NGMRPDTTAE SLARLKPAFD PFGSVTAGNS SQITDGACWL LLASEQGLKK HGLTPIARLA
HTAWAALDPS MMGLGVTLSS TAILKQRGWG LDDIDYWEIN EAFAGQVLAC LNAWADDAYC
REQLGLEQAL GELDMTRLNV DGGAIGLGHP IGASGARIVL HLIHVLRRHQ TRRGIASLCI
GGGQGGAMLV ENIES
//
