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Database: UniProt
Entry: I0AJX3_IGNAJ
LinkDB: I0AJX3_IGNAJ
Original site: I0AJX3_IGNAJ 
ID   I0AJX3_IGNAJ            Unreviewed;       392 AA.
AC   I0AJX3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN   Name=atoB {ECO:0000313|EMBL:AFH49280.1};
GN   OrderedLocusNames=IALB_1572 {ECO:0000313|EMBL:AFH49280.1};
OS   Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS   Mat9-16).
OC   Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC   Ignavibacteriaceae; Ignavibacterium.
OX   NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH49280.1, ECO:0000313|Proteomes:UP000007394};
RN   [1] {ECO:0000313|EMBL:AFH49280.1, ECO:0000313|Proteomes:UP000007394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC   {ECO:0000313|Proteomes:UP000007394};
RX   PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA   Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA   Bryant D.A.;
RT   "Complete genome of Ignavibacterium album, a metabolically versatile,
RT   flagellated, facultative anaerobe from the phylum Chlorobi.";
RL   Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH49280.1; -; Genomic_DNA.
DR   RefSeq; WP_014560433.1; NC_017464.1.
DR   AlphaFoldDB; I0AJX3; -.
DR   STRING; 945713.IALB_1572; -.
DR   GeneID; 78243240; -.
DR   KEGG; ial:IALB_1572; -.
DR   PATRIC; fig|945713.3.peg.1573; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_0_1_10; -.
DR   OrthoDB; 9764892at2; -.
DR   Proteomes; UP000007394; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
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:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 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; PS00098; THIOLASE_1; 1.
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:UP000007394};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AFH49280.1}.
FT   DOMAIN          4..261
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          268..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        347
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        377
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   392 AA;  41609 MW;  266787BAF5117BD9 CRC64;
     MKKVVIVSAK RTPIGSFNGS LSSFTAGQLG SIAIKAVVED SKIDVNLIDE VIMGNVLMGG
     QGQAPARQAA LFAGLPNKVE CMTINKMCGS GLKAVMIAQQ AILAGDADII IAGGQESMTN
     TPYILPKARN GYRLGHGEVQ DLIVLDGLWD VYNQIHMGSC AEVCAKEFKF SREELDEFAI
     NSYKRAINAT QTGRFKDEII PVKVAGKKGD TIVDKDEEPE RVIFEKIPSL KPVFEKDGVV
     TAANASSIND GAAALLVMSE EKAKELGLKP LVELVAQASA AKAPIDFTTA PADAINKVLK
     KANMSVNDID LYEINEAFAV VSLAVNKLLN LSVDKVNVNG GAVALGHPIG ASGARILTTL
     IYEMKKRNVE YGLASLCIGG GEASALIVKN YQ
//
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