ID   HBOH_CUPMC              Reviewed;         722 AA.
AC   Q1LLY7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-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=Rmet_1960;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(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; CP000352; ABF08839.1; -; Genomic_DNA.
DR   RefSeq; WP_011516685.1; NC_007973.1.
DR   AlphaFoldDB; Q1LLY7; -.
DR   STRING; 266264.Rmet_1960; -.
DR   EnsemblBacteria; ABF08839; ABF08839; Rmet_1960.
DR   KEGG; rme:Rmet_1960; -.
DR   eggNOG; ENOG502Z8QU; Bacteria.
DR   HOGENOM; CLU_420258_0_0_4; -.
DR   OMA; NPEKDWG; -.
DR   OrthoDB; 865015at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000002429; Chromosome.
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; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT   CHAIN           37..722
FT                   /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT                   /id="PRO_5000118750"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ   SEQUENCE   722 AA;  73917 MW;  911C2C8140F5A68D CRC64;
     MQQRHLSQSA HSHGHGTRRA HRRNTIAIAV ATLAVAACGG FGTNGSGGNT GPNVKPAFIS
     GPVGVKSYDG NTDDLLTAGL GKDGLAAAAP AFANPNAPTA VELRRNAIWA NYRAIVDVQA
     AGGYGSLYGP NVDAKGNVTT GQGKVPGTEY IAFTDDGSGR QNVTVMAQVP DGFDVKHPCI
     ISATSSGSRG VYGGIAVGEW GLKHNCAVAY TDKGTGAAPH DLGSDTVPLI DGTRQTRAGA
     GTQAQFAAQP GASETLAGFN SSTPHRLAFK HAHSQQNPEA NWGANTLQAI QFTLWAVNDK
     FGRTNTDGMR QATFTPANVL VIASAISNGG GAAIAAAEQD TGGLIDGVAV GEPNVNLPPT
     AGVVVKRGGV PVAASGKHLY DYTTIANLYQ LCASQDASLG NAPFAKTAGQ AALNRCASLA
     AKKMIAGGST SAQATSALDA LHRAGWEPES DDLFASLSAL EVGSSISVTY ANAYARASVT
     DRLCHYSFSS PGSPPQANPV TAPAAALAGL FSTGNGIPPT TAVTLMNDAN PSGAMRDFTS
     ISPSTKLADG NVDGALCLRG LLDTRNPALM TGIGQTYRTG NLGGRPSVIV QGRSDGLLPV
     NHTSRPYLGL NKHVEGASSR LSYIEVTNGQ HFDGFIDVIP GYAKRYIPMH VYVNRALDAV
     YANLRDGTPL PPSQVVRTTP RGGADTDTVG PRIQPSNVPP IAATPAAGDA ITVTGSTVDV
     PN