ID D6V0L1_9BRAD Unreviewed; 252 AA.
AC D6V0L1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Acetyl-CoA C-acyltransferase {ECO:0000313|EMBL:EFI53241.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:EFI53241.1};
GN ORFNames=AfiDRAFT_1228 {ECO:0000313|EMBL:EFI53241.1};
OS Afipia sp. 1NLS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=666684 {ECO:0000313|EMBL:EFI53241.1, ECO:0000313|Proteomes:UP000004041};
RN [1] {ECO:0000313|EMBL:EFI53241.1, ECO:0000313|Proteomes:UP000004041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLS2 {ECO:0000313|EMBL:EFI53241.1,
RC ECO:0000313|Proteomes:UP000004041};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Prakah O.,
RA Elkins J.G., Brown S.D., Palumbo A.V., Hemme C., Zhou J., Watson D.B.,
RA Jardine P.M., Kostka J.E., Green S.J., Woyke T.J.;
RT "The draft genome of Afipia sp. 1NLS2.";
RL Submitted (MAY-2010) 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:EFI53241.1}.
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DR EMBL; ADVZ01000001; EFI53241.1; -; Genomic_DNA.
DR RefSeq; WP_002718161.1; NZ_ADVZ01000001.1.
DR AlphaFoldDB; D6V0L1; -.
DR eggNOG; COG0183; Bacteria.
DR Proteomes; UP000004041; Unassembled WGS sequence.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase 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; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:EFI53241.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EFI53241.1}.
FT DOMAIN 1..100
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 111..250
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 252 AA; 27377 MW; 9A92B564A1C4DEE9 CRC64;
MGEHMEETAK EWHISREAQD AWALKGHQRA VAGWNSGFFD DLVIKLPELE CDSNPRADTS
SEKLAALKPA FDKRSGQGTL TAGNSSPITD GAAGCWIANE AGLDRLPSNT PYLRLVDYEV
AAVDHHTEGL LMAPSYAIPR LLARHGLRFD DIHLWEIHEA FAAQVLANVA AIERRDWIRS
KTGVDADFGT FRWDRVNPNG GSVAIGHPFA ATGARDLSQA VKELWSRPAG SRGIISVCAD
GGQGTVALLE RV
//
