ID A0A1G5ET47_9PROT Unreviewed; 399 AA.
AC A0A1G5ET47;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=SAMN05216308_10750 {ECO:0000313|EMBL:SCY29951.1};
OS Nitrosospira sp. Nsp13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=1855332 {ECO:0000313|EMBL:SCY29951.1, ECO:0000313|Proteomes:UP000198731};
RN [1] {ECO:0000313|EMBL:SCY29951.1, ECO:0000313|Proteomes:UP000198731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nsp13 {ECO:0000313|EMBL:SCY29951.1,
RC ECO:0000313|Proteomes:UP000198731};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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; FMVD01000007; SCY29951.1; -; Genomic_DNA.
DR RefSeq; WP_074630630.1; NZ_FMVD01000007.1.
DR AlphaFoldDB; A0A1G5ET47; -.
DR OrthoDB; 6139495at2; -.
DR Proteomes; UP000198731; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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:SCY29951.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SCY29951.1}.
FT DOMAIN 9..268
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 277..397
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 95
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 399 AA; 41873 MW; 72929366F26261DE CRC64;
MSKQIQDAYI VAAVRTPVGK APRGMFKTVR PDDMLAHVLK AAMAQCEGLD PAAIEDVIAG
CAMPEAEQGM NVARIGLLLA GLPDSVPGMT INRFCASGLQ AVAIAADRIR LGEADVMIGA
GTESMSMVPM TGNKMSLDPA IFARNENVAI AYGMGITGEK VAQRWQVSRE AQDEFAVTSH
ARALEAIKMG EFRQEIAPYP VEEKLPDLVT HEVRNVSTIR DTDEGPRPGT NPQTLATLRP
VFAAGGSVTA GNSSQMSDGA GAVIVASEAA LKRFNLTPIG RFMGFAVAGV PPEIMGIGPI
KAIPKVLKQI GLSQDDLDWI ELNEAFAAQS LAVINDLGLD RAKVNPLGGA IALGHPLGAT
GAIRVATLLH GLRRHNQKYG MVTMCVGTGM GAAGVFEAL
//
