ID   HBOH_BURL3              Reviewed;         696 AA.
AC   Q39J35;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 75.
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   Flags: Precursor;
GN   OrderedLocusNames=Bcep18194_A3932;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000255|HAMAP-
CC       Rule:MF_01906}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_01906}.
CC   -!- SIMILARITY: Belongs to the D-(-)-3-hydroxybutyrate oligomer hydrolase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01906}.
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DR   EMBL; CP000151; ABB07531.1; -; Genomic_DNA.
DR   RefSeq; WP_011351114.1; NC_007510.1.
DR   AlphaFoldDB; Q39J35; -.
DR   EnsemblBacteria; ABB07531; ABB07531; Bcep18194_A3932.
DR   GeneID; 45093837; -.
DR   KEGG; bur:Bcep18194_A3932; -.
DR   PATRIC; fig|482957.22.peg.806; -.
DR   HOGENOM; CLU_420258_0_0_4; -.
DR   OMA; NPEKDWG; -.
DR   OrthoDB; 865015at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000002705; Chromosome 1.
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   3: Inferred from homology;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT   CHAIN           21..696
FT                   /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT                   /id="PRO_0000314425"
FT   ACT_SITE        309
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ   SEQUENCE   696 AA;  71763 MW;  DB2E5033D303D772 CRC64;
     MTRLGWGRRM VFGAALAAVA ILGACNGDES AERNRLPGFV SGSVRTTAYD GASDDLLTAG
     LGKTGLGSAS APGFANAARP TSAELRRLAI WSNYRALVDM SANGGYGRFW GPNVDLDGND
     TLGEGKIPGT EYLAYSDDGS GSKNVTLLVQ VPAGFNPAQP CIVTATSSGS RGVYGAISAA
     GEWALKRGCA VAYNDKGGGN GAHELMSDTI TLIDGTLANA VLAGTSSLFT ANVTSGDLAT
     FNSRFPNRYA FKHAHSQQNP EQDWGHVTLQ SVEFAYWALN EQFGPLIDGS RHGVRYRAGD
     IMTIAASVSN GGGASLAAAE QDTRGWITAV VVGEPQINVR MAPNVVVRSG GQPVPSFGRP
     LADYATLANL LEPCAAASAS LAGAPYLSAL PVATTQSIRT QRCATLAAAG LVSGADTQSQ
     AADALAQLHA AGYLADSDLL QAPMWDSQAI PAIAVTYANA YTRSRVTDNL CNFSFATTNP
     ATGAVAAPAT SPMPAVFGVG NGVPPTAGID LVFNTGAGVD HRLATPDASF AGALCLRQLW
     TNGMLGMPAN VDAVRVNANL QGKPAIIVQG RSDSLVPVNH ASRAYVAQNG ISEAGRSQLV
     FYEVTNGQHF DAFLPVPGFD TRFVPVHYYN LQALNLMWKH LKNGAPLPPS QVIRTVPRGG
     TPGAAPALTS ANLPPISAAP GANAITVGAG AIDVPL