ID A0A087NFI8_9SPHN Unreviewed; 418 AA.
AC A0A087NFI8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acetyl-CoA acyltransferase {ECO:0000313|EMBL:KFL47891.1};
GN ORFNames=IL54_3318 {ECO:0000313|EMBL:KFL47891.1};
OS Sphingobium sp. ba1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1522072 {ECO:0000313|EMBL:KFL47891.1, ECO:0000313|Proteomes:UP000029094};
RN [1] {ECO:0000313|EMBL:KFL47891.1, ECO:0000313|Proteomes:UP000029094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ba1 {ECO:0000313|Proteomes:UP000029094};
RA Manzari C., Chiara M., Costanza A., Leoni C., Picardi E., Trotta M.,
RA Volpicella M., D'Erchia A.M., Horner D.S., Pesole G., Ceci L.R.;
RT "Draft genome sequence of a Kanamycin and Nickel resistant bacterium
RT Sphingobium species.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFL47891.1}.
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DR EMBL; JPPQ01000069; KFL47891.1; -; Genomic_DNA.
DR RefSeq; WP_037476728.1; NZ_JPPQ01000069.1.
DR AlphaFoldDB; A0A087NFI8; -.
DR PATRIC; fig|1522072.3.peg.2051; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000029094; Unassembled WGS sequence.
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; -; 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; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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:KFL47891.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KFL47891.1}.
FT DOMAIN 5..236
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 296..417
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 374
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 404
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 418 AA; 43591 MW; 2FC0ABA2F1B29849 CRC64;
MAEAFIIDAV RTPRSFGKLG KGALSHLHPQ HVAATVLRAI RDRNGIDTAD VDDVIWGTSA
QMGLQGGDMG RMAALDAGYD VRASGVTLDR FCGSGLTATN LAAAQIMAGM EDLVVAGGTE
MMSHVMSYGQ SLREAGVPSV GGLGTGNLRL QAKHPQSNQG VAADAIAAME GITREQLDAF
GAESQRRAGI AIKEGRFARS TVPVVDDDGA VILDHEEYPR PDTTAEQLAQ LKPAFAAFLD
MPSRADGPTF RQLINQTYPD LAITPLHHAG TSSGVVDGAA ALLLASADYA QRHGLTPRAR
VVATANMGDC PTLMLNGPVP AARKVLAKAG LRVEDIDVFE VNEAFAVVTE KFIRDLGIDR
AKLNPNGGAI ALGHPIGATG AVLIGTALDE LERTGGRYGL ITMCAAGGMA PAIIIERV
//
