ID   HBOH_BURCM              Reviewed;         695 AA.
AC   Q0BHU5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Bamb_0719;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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; CP000440; ABI86278.1; -; Genomic_DNA.
DR   RefSeq; WP_011656103.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BHU5; -.
DR   STRING; 339670.Bamb_0719; -.
DR   EnsemblBacteria; ABI86278; ABI86278; Bamb_0719.
DR   GeneID; 44691403; -.
DR   KEGG; bam:Bamb_0719; -.
DR   PATRIC; fig|339670.21.peg.875; -.
DR   eggNOG; ENOG502Z8QU; Bacteria.
DR   OMA; NPEKDWG; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000000662; 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..17
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT   CHAIN           18..695
FT                   /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT                   /id="PRO_0000314414"
FT   ACT_SITE        308
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ   SEQUENCE   695 AA;  71704 MW;  851CE01B07CF30B2 CRC64;
     MTTHGWGTRI LLGAALAALT LLGGCNDADS GERNRLPGFV SGSVRTTAYD GTSDDLLTAG
     LGKTGLASTA PAFANPSRPT SAELRRLAIW SNYRALVDMS ANGGYGRFWG PNVDLDGNAT
     LGEGKIPGTE YLAYSDDGSG RKNVTLLVQV PASFDPKQPC IVTATSSGSR GVYGAISAAG
     EWGLKRGCAV AYNDKGGGNG AHELGSDTIT LIDGTLANAV LAGNASLFTA NVTSGDLAAF
     NGRFPNRYAF KHAHSQQNPE QDWGHATLQA VEFAYWALNE QFGPVLDSSH HGVRYHPGDI
     TTIAASVSNG GGAALAAAEQ DTRRWITAVV VGEPQVNVRM SPNAIVREGG QPAPSFGRPL
     ADYATLANLL QPCAAASASL AGEPYLSGLP AATTQSIRTQ RCATLAAAGL VSGADTQSQA
     ADALAQLHAA GYLADSDLLQ ASMWDSQAIP AIAVTYANAY TRSRVTDNLC NFSFATTSAP
     TGTVASPAAS PMPAIFGVGN GVPPTGGIDL VFNTGAGVDH RLATPDASFA GALCLRQLWT
     NGMLDMPANV DAVRVNANLQ GKPAIIVQGR SDALVPVNHA SRAYVAQNSI SEGARSQLVF
     YEVTNGQHFD AFLPVAGFDT RFVPVHYYNV QALNLMWRHL KNGAALPPSQ VIRTVPRGGT
     PGAAPALTSA NLPPIATSPG ANAITAGAGA IDVPL