ID E4TJR6_CALNY Unreviewed; 392 AA.
AC E4TJR6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ADR19262.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ADR19262.1};
GN OrderedLocusNames=Calni_1354 {ECO:0000313|EMBL:ADR19262.1};
OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Calditerrivibrionaceae.
OX NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR19262.1, ECO:0000313|Proteomes:UP000007039};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19672;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A.,
RA Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Calditerrivibrio nitroreducens DSM
RT 19672.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADR19262.1, ECO:0000313|Proteomes:UP000007039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1
RC {ECO:0000313|Proteomes:UP000007039};
RX PubMed=21475587; DOI=10.4056/sigs.1523807;
RA Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Land M.;
RT "Complete genome sequence of Calditerrivibrio nitroreducens type strain
RT (Yu37-1).";
RL Stand. Genomic Sci. 4:54-62(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; CP002347; ADR19262.1; -; Genomic_DNA.
DR RefSeq; WP_013451474.1; NC_014758.1.
DR AlphaFoldDB; E4TJR6; -.
DR STRING; 768670.Calni_1354; -.
DR KEGG; cni:Calni_1354; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_0; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000007039; 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; 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:SF138; ACETYL-COA C-ACETYLTRANSFERASE; 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 ECO:0000313|EMBL:ADR19262.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007039};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ADR19262.1}.
FT DOMAIN 4..259
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..390
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; 42126 MW; CEA9633456AADEA9 CRC64;
MKNVYLIDGI RTPFGSFGGA LSDIPAPELA SILIKELQQK YNLPSDAANE VIIGQVIQGG
SRQAPARQAM RLAGLSDSVH AMTVNKVCGS GLKSVMLATQ SILLGDSSLV YAGGMENMSM
APFAMDKARF GYRMGHSTFF DLMIYDALQD PYSGKHMGEI TEESIKKNGI TREEQDNYAI
RSYTLAQSAI ENGTIRSEIL PVIKKTKKGE QIIDKDEDPF KGDIAKLESL KPVFAKDGSI
TAGNASKIND GAAITLIADD DAVKKYGFQP KIRIVAYSTN SIHPSDFGEA PIGAIEKVVE
KAQLNLDQID LFEINEAFAA VPLMAIKKLK LDINKVNVNG GAVAFGHPVG ASGARLLITL
AREMIQKNKK YGIATLCIGG GEAVAVLIEK IN
//
