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Database: UniProt
Entry: A0A109BPR0_HYPSL
LinkDB: A0A109BPR0_HYPSL
Original site: A0A109BPR0_HYPSL 
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
//
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