ID   HBOH_BURM9              Reviewed;         699 AA.
AC   A2S9Q3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=BMA10229_A2720;
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000546; ABN03220.1; -; Genomic_DNA.
DR   RefSeq; WP_011832341.1; NC_008836.1.
DR   AlphaFoldDB; A2S9Q3; -.
DR   EnsemblBacteria; ABN03220; ABN03220; BMA10229_A2720.
DR   GeneID; 56594963; -.
DR   KEGG; bml:BMA10229_A2720; -.
DR   HOGENOM; CLU_420258_0_0_4; -.
DR   OMA; NPEKDWG; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000002283; Chromosome I.
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; IPR029058; AB_hydrolase.
DR   InterPro; IPR016582; OHBut_olig_hydro_put.
DR   Pfam; PF10605; 3HBOH; 1.
DR   PIRSF; PIRSF011409; HObutyrate_olig_hydrol; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT   CHAIN           34..699
FT                   /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT                   /id="PRO_0000314416"
FT   ACT_SITE        311
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ   SEQUENCE   699 AA;  71661 MW;  B35FE03CA626C120 CRC64;
     MTAIRGGSRR APGLALALLG GVLLGACHGD ENAQVNALPG FVSGSVRKTA YDGASDDLLT
     AGLGKTGLGS DTRPGFANPA QPSAAELRRL AIYSNYRALV DITPNGGYGR FWGPNVDLAG
     NDTLGEGKIA GTEYLAYSDD GSGRKNVTLL VQVPASFDPA NPCIVTATAS GSRGVYGAIA
     AAGEWGLKRG CAVAYNDKGG GNGAHEIGTG VVTLIDGTLA TASSAGSSSL FTASESSSTL
     AAFNSAFPNR YAYKHAHSQQ NPEQDWGLVT LQAVEFAYWA LNEQFGPVVD GTRHGIRYRP
     GDITTIAASV SNGGGSALAA AEQDTRGWIT AVVVGEPQIN VRMTPGVTVE QGGAPVPSFG
     RPLADYATLA NLLQPCAAAA VAATGAPYLS ALPMGVTQSI RTQRCATLAA AGLVSGADTA
     SQASDALAQL YAAGYLADSD LLQAPMWDSQ AMPAIAVTYA NAYTRSRVTD NLCNFSFATT
     NPVTGAVAAP AVSPMTNLFG AGNGVPPTNG INLVFNGASG GVDHRLATPD ASFAGAFCLR
     QLWTANQLGI GTNVDAVRVA ANLQHKPAII VHGRSDALVP VNHASRAYVA QNSATEGRAS
     QLSFYEVTNG QHFDAFLSVP GFDTRFVPVH YYDEQALNLM WNHLKSGAPL PPSQVIRTVP
     RGGVPGAAPA LSTANLPPIV QSPGANAIAV NAGVIDVPL