ID   HBOH1_RALPI             Reviewed;         722 AA.
AC   O05690;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=D-(-)-3-hydroxybutyrate oligomer hydrolase {ECO:0000255|HAMAP-Rule:MF_01906};
DE            Short=3HB-oligomer hydrolase {ECO:0000255|HAMAP-Rule:MF_01906};
DE            Short=3HBOH {ECO:0000255|HAMAP-Rule:MF_01906};
DE            EC=3.1.1.22 {ECO:0000255|HAMAP-Rule:MF_01906};
DE   AltName: Full=Extracellular 3HB-oligomer hydrolase;
DE            Short=e3HBOH;
DE   Flags: Precursor;
OS   Ralstonia pickettii (Burkholderia pickettii).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, ACTIVITY
RP   REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=A1;
RX   PubMed=8981982; DOI=10.1128/jb.179.1.72-77.1997;
RA   Zhang K., Shiraki M., Saito T.;
RT   "Purification of an extracellular D-(-)-3-hydroxybutyrate oligomer
RT   hydrolase from Pseudomonas sp. strain A1 and cloning and sequencing of its
RT   gene.";
RL   J. Bacteriol. 179:72-77(1997).
CC   -!- FUNCTION: Participates in the degradation of poly-3-hydroxybutyrate
CC       (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase,
CC       hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-
CC       oligomers) into 3HB-monomers. {ECO:0000255|HAMAP-Rule:MF_01906,
CC       ECO:0000269|PubMed:8981982}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxybutanoate dimer + H2O = 2 (R)-3-hydroxybutanoate +
CC         H(+); Xref=Rhea:RHEA:10172, ChEBI:CHEBI:10979, ChEBI:CHEBI:10983,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378; EC=3.1.1.22;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01906};
CC   -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP).
CC       {ECO:0000269|PubMed:8981982}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.18 mM for 3HB-dimer {ECO:0000269|PubMed:8981982};
CC         KM=0.17 mM for 3HB-trimer {ECO:0000269|PubMed:8981982};
CC         Vmax=25 umol/min/mg enzyme with 3HB-dimer as substrate
CC         {ECO:0000269|PubMed:8981982};
CC         Vmax=30 umol/min/mg enzyme with 3HB-trimer as substrate
CC         {ECO:0000269|PubMed:8981982};
CC       pH dependence:
CC         Optimum pH is 7-8.5. {ECO:0000269|PubMed:8981982};
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000255|HAMAP-
CC       Rule:MF_01906}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_01906,
CC       ECO:0000269|PubMed:8981982}.
CC   -!- SIMILARITY: Belongs to the D-(-)-3-hydroxybutyrate oligomer hydrolase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01906}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20331.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR   EMBL; D85373; BAA20331.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; O05690; -.
DR   UniPathway; UPA00863; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0047989; F:hydroxybutyrate-dimer hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01906; 3HBOH; 1.
DR   InterPro; IPR016582; OHBut_olig_hydro_put.
DR   Pfam; PF10605; 3HBOH; 1.
DR   PIRSF; PIRSF011409; HObutyrate_olig_hydrol; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT   CHAIN           26..722
FT                   /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT                   /id="PRO_0000314419"
FT   ACT_SITE        319
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ   SEQUENCE   722 AA;  73826 MW;  FC97DCDA878CB928 CRC64;
     MKTMQGKGSG RRLRGALLVT MAASGAIGLA GCGGSNDNTT TTTPTNVKPS FVGTVTVTHF
     DGVSDDLLTA GLGAAGLASA TAPTVANATA PTAAELRRLA IYNNYRALVD TNAKGGYGTL
     YGPNVDASGN VTSGSGMVPG VEYVAYSDDG SGQQNVVLLV QIPDAFDAAN PCIITATSSG
     SRGIYGAIST GEWGLKRKCA VAYTDKGTRA GPHDLATDTV PLQDGTRTTR AAAGSKAQFA
     APLTDTQLAA FNLATPNRLA FKHAHSQRNP EKDWGRFTLQ AVQFAFWAIN DKLSGGSAPN
     GSALAVRPDN TIVIASSVSN GGGAAIAAAE QDTTHLIDGV AVGEPGLNLP ASANVQVQRG
     GVTLPVTGKP LFDYVSYANA FRLCAALSSS VSGAPTQSFF AGNIGWPASV QANRCAALHA
     NGLLSSTTTA AQADEALQKM RTYGWEPESD LVHASMAYFE IDPSVATTFG NALARASVLD
     NLCNFSFAAV DTSFHPTTVN ATALAQLAST GNGIPPTTGV QLINNLAQGG ATQSKQSVDS
     SGTQAANLDG ALCLRKLLTG ADAASQALQL GISQTLRTGN LGGRPALIVQ GRNDALLPVN
     HGARPYLGLN AQVDTSSKLS YIEVTNAQHF DGFIDLVPGY DTLFVPLVLY EQRALDAVYA
     NLKNGTPLPP SQVVRTTPRG GTAGSAPAIA ATNVPNFTNT PAVADRISVS VSGGVATVSV
     PN