ID A0A078M0W9_9STAP Unreviewed; 394 AA.
AC A0A078M0W9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Probable acetyl-CoA acyltransferase {ECO:0000256|ARBA:ARBA00014048};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN Name=fadA {ECO:0000313|EMBL:CEA01008.1};
GN ORFNames=BN1048_01199 {ECO:0000313|EMBL:CEA01008.1};
OS Jeotgalicoccus saudimassiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Jeotgalicoccus.
OX NCBI_TaxID=1461582 {ECO:0000313|EMBL:CEA01008.1, ECO:0000313|Proteomes:UP000044136};
RN [1] {ECO:0000313|EMBL:CEA01008.1, ECO:0000313|Proteomes:UP000044136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13MG44_air {ECO:0000313|EMBL:CEA01008.1,
RC ECO:0000313|Proteomes:UP000044136};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-2014) 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; CCSE01000001; CEA01008.1; -; Genomic_DNA.
DR RefSeq; WP_035809425.1; NZ_CCSE01000001.1.
DR AlphaFoldDB; A0A078M0W9; -.
DR STRING; 1461582.BN1048_01199; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_1_1_9; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000044136; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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 Reference proteome {ECO:0000313|Proteomes:UP000044136};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 5..261
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..391
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 92
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 41641 MW; C1CEA571B2F8DB6A CRC64;
MQDAYIVAYG RSAAGRAKGG AMFHDRPDEV AAQVLKGVLK RVDGKFSPDM VQDVIVGNSF
PEGLQGQNIA RSIALLAGMP NEVPGQTVNR YCSSGLQTIA IAANQIMAKQ ADVLVAGGVE
LMSAVPMGGN EPTNSPVLQD EDSGVSYPMG LTAEMVAEEF KVSREDQDAY AVQSHQRAKA
ALDAGRFEDE IIPVEVNKVS YNEEGPVVSK DEFKIDEHIR PDTNMEGLAK LRTVFKADGT
VTAGTSAPLT DGAGFVVLMS GEKVKELGVT PIARFVGFKA VGVDPKIMGI GPAYAIPEVL
EQAGLTVDDM DLIELNEAFA SQTVASIRKA GLDIEKTNVN GGAISLGHPL GASGAMLTAR
LLSEMKRRPE SKYGMVTMCI GVGMGAAGIF EYVR
//
