ID I0JID2_HALH3 Unreviewed; 390 AA.
AC I0JID2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:CCG43900.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:CCG43900.1};
GN OrderedLocusNames=HBHAL_1530 {ECO:0000313|EMBL:CCG43900.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG43900.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG43900.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(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; HE717023; CCG43900.1; -; Genomic_DNA.
DR RefSeq; WP_014641807.1; NC_017668.1.
DR AlphaFoldDB; I0JID2; -.
DR STRING; 866895.HBHAL_1530; -.
DR KEGG; hhd:HBHAL_1530; -.
DR PATRIC; fig|866895.3.peg.528; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_9; -.
DR Proteomes; UP000007397; Chromosome.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase 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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 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:CCG43900.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007397};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:CCG43900.1}.
FT DOMAIN 7..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 267..389
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 390 AA; 40826 MW; FEAA23EFC62AA28F CRC64;
MTERDAVIVS AVRTAIGKQG GTLAKVPAHV LGAEVIKEAV KRAGVDVDMI EDVIMGNVLS
GGGNVARLSA LQSGLSINLP GLTVDRQCGS GLNAIYLAAQ AIRAGSGDVY VAGGTESMSQ
APYLMERPER AFSPVPPKFK KSQLAPKEIG DPPMGITAEN LAEKYSIPRE EQDQFAQQSQ
QRMGMAIEEG RFEEQIVPLE IPVRKGAPIE FKVDEHPRPD STVEGMAKLR PAFLEEGTVT
AGNSSGLNDA ASALMVMSRE KADEAGLTPL ATVKACAVAG VDPNIMGIGP VPATQKVLEE
TGLGLDDMDI IEINEAFAAQ VLACNKEMEM DLEKVNVNGG AIAHGHPLGA TGAILATKAI
YELKRSGGQY ALVTACIGGG QGIAMILERG
//
