ID   HBOH_CUPPJ              Reviewed;         707 AA.
AC   Q46ZT8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Reut_A1981;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ61345.1; -; Genomic_DNA.
DR   RefSeq; WP_011298143.1; NC_007347.1.
DR   AlphaFoldDB; Q46ZT8; -.
DR   STRING; 264198.Reut_A1981; -.
DR   ESTHER; cupnj-hboh; OHBut_olig_hydro_put.
DR   EnsemblBacteria; AAZ61345; AAZ61345; Reut_A1981.
DR   KEGG; reu:Reut_A1981; -.
DR   eggNOG; ENOG502Z8QU; Bacteria.
DR   HOGENOM; CLU_420258_0_0_4; -.
DR   OMA; NPEKDWG; -.
DR   OrthoDB; 865015at2; -.
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   3: Inferred from homology;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT   CHAIN           25..707
FT                   /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT                   /id="PRO_0000314430"
FT   ACT_SITE        311
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ   SEQUENCE   707 AA;  73456 MW;  7FB7E8A64C2D7F1A CRC64;
     MHHDNFRRLG NAAFAAAAAL LAVACGGGDS SDGNTNPNIK PANIGTVTIQ AYDGATDDLL
     TAGLGKDGLA SATAPVPASP NSPTAAELRR YAIYTNYRAI VDTTAGGGFG SLYGPNVDAQ
     GNVTTGQGKI AGVEYLAFSD DGSGQENVTM LVQIPNTFNQ SKPCMITATS SGSRGVYGAI
     AVGEWGLKRG CAVAYTDKGT GAAPHDLDTD TVPLIDGTRT TRSAAGTNAQ FAARPGILSL
     ADFTAQVPHR LAFKHAHSQR NPEKDWGKFT LQAIEFGIWA INDRFGTVAS NGVRQRTLAK
     SKIVVIASSV SNGGGAAVAA AEQDTDGLID GVAVAEPNLN LPPNASILVK RGSKPVNASG
     RLLYDYITTA NLLQLCASQA TALVNAPAFA TNQFYISRCQ TLVDNKLISG TTVSDQAASA
     LDQLHLAGWE PESDALHPSL SLFDTAASIA VTYANSYARA SVTDRLCGYS FAATLADFKP
     AAIAPSVLAS MFATGNGVPP TSTVQLINDR DLQHGPFMNG QSVSASNNRA DANFDGAKCL
     RDLLTGTDSQ AQALQSGVSQ IQRSGNLHGK PALIVHGRSD GLLPVNHTSR PYLGFNRQQE
     GAASKLSYIE VENAQHFDAF IGAVSGYSNR YVPLHLYLIR ALDAVYDNLT TGKALPPSQV
     VRTIPRGGAT NTTTAPTLLP VNVPPISASP DAANQIAAST GSVDVPD