ID   HBOH_PARXL              Reviewed;         707 AA.
AC   Q13Q76;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Bxeno_B0795; ORFNames=Bxe_B2223;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000271; ABE33763.1; -; Genomic_DNA.
DR   RefSeq; WP_011491122.1; NZ_CP008762.1.
DR   AlphaFoldDB; Q13Q76; -.
DR   STRING; 266265.Bxe_B2223; -.
DR   ESTHER; parxl-hboh; OHBut_olig_hydro_put.
DR   EnsemblBacteria; ABE33763; ABE33763; Bxe_B2223.
DR   KEGG; bxb:DR64_4554; -.
DR   KEGG; bxe:Bxe_B2223; -.
DR   PATRIC; fig|266265.5.peg.5493; -.
DR   eggNOG; ENOG502Z8QU; Bacteria.
DR   OMA; NPEKDWG; -.
DR   OrthoDB; 865015at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000001817; Chromosome 2.
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..32
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT   CHAIN           33..707
FT                   /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT                   /id="PRO_0000314427"
FT   ACT_SITE        321
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ   SEQUENCE   707 AA;  72305 MW;  8ED26586BDA56018 CRC64;
     MASVFKVRSA SGHVPVVRTL AAMMAVTVVL TACHGGGDNH PPPQANVLPA FITASSVRTQ
     FYDGNTDDLL TAGLGKTGLA SATAPAIANA AQPTAAELRR LAIWSNYRAL VDMTANGGYG
     RFWGPNVDLN GNDTLGEGKI AGKEYLAFAD DGSGTQNVTV LVQIPASFNP DQPCIVTATS
     SGSRGVYGAI SAAGEWGLKR GCAVAYTDKG SGNGAHELSS SLVTLIDGTL QNATAAGKAS
     LFTANLGNTD LASYNSRFPN RYAFKHAHSQ QNPEKDWGRN TLQAIQFAYW ALNDSYGTLN
     GSTRNVRYTS GSITTIAASV SNGGGASLAA AEQDTSGLIT AVVVGEPQIN LRLPAQVSVA
     QGGVPVGAFG KPLADYMTLA NMLQPCAALA PAAAGAPYLT ALPGATTTSI RTARCASLAA
     AGVIAGADAT TQATNALALL HQNGYQTDSD LLQAPMWDSQ AVPAVAVTYA DAYAKASVTA
     NLCNFSFGTT NAAGTAGVTP AVSPMLTVFG NGNGVPPTNG INLVFNSGAG AADHRLATAD
     GSYAGASCLR TLWTNGTLTG SVDAIRVNAN LHGKPAIIVQ GRADALVPIN HASRPYLGLN
     QLSEGAASRL SFYEVTNAQH FDAFLGVAGF DSRFVPLHYY NLQALNLMWS HLKNGTPLPP
     SQVIHTVPRG GTPGAAPALT TANLPPIVAS PGINAITAAN GAVNVPN