ID A0A109BPR0_HYPSL Unreviewed; 434 AA.
AC A0A109BPR0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=3-ketoacyl-CoA thiolase Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KWT72425.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:KWT72425.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KWT72425.1};
GN ORFNames=APY04_0116 {ECO:0000313|EMBL:KWT72425.1};
OS Hyphomicrobium sulfonivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT72425.1, ECO:0000313|Proteomes:UP000059074};
RN [1] {ECO:0000313|EMBL:KWT72425.1, ECO:0000313|Proteomes:UP000059074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDL6 {ECO:0000313|EMBL:KWT72425.1,
RC ECO:0000313|Proteomes:UP000059074};
RA Albers P.;
RT "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT consortium.";
RL Submitted (OCT-2015) 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:KWT72425.1}.
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DR EMBL; LMTR01000011; KWT72425.1; -; Genomic_DNA.
DR RefSeq; WP_068458935.1; NZ_LMTR01000011.1.
DR AlphaFoldDB; A0A109BPR0; -.
DR STRING; 121290.APY04_0116; -.
DR PATRIC; fig|121290.4.peg.1438; -.
DR OMA; HCEDMAK; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000059074; Unassembled WGS sequence.
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; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
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 PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KWT72425.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059074};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KWT72425.1}.
FT DOMAIN 8..276
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 300..423
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 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 411
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 434 AA; 45826 MW; 1AFE119482B7EA6A CRC64;
MQRFMRRVAV IGGARIPFCR SNTFYADLTN LDLMTGALNA LIDRYGLKGQ HIDEVVGGAV
ITHSKDFNLT REAVLSTALA PSTPGITMMQ ACGTSLQAAL GSAAKIATGD IDCAIAVGSD
TTSDAPIVVS KKLAKRLTQA AQRKTFMDKL KTFKGFAPGE LVPQAPANAE PRTGLSMGEH
AEMMAREWGI TRDAQDRFAL ESHLKAAEAY RSGYMDDIVT PFAGVFRDNN IRADASIDKL
SSLKASFDKS GKGTLTAGNS TPLTDGAAAV LLASEDWAEK HGLPVAAYLT YSQSAANDFV
AGDGLLMAPT IAVSRMLDRA GLKLQDFDFY EIHEAFAAQV LATLKAWEDP TYCRQVLGRP
EAMGAIDPAK INVHGSSIAL GHPFAATGAR IVGNMAKLLA GHHGRGLISI CTAGGMGVAA
ILESKDAAEI HQAA
//