HBOH_BURMS
ID HBOH_BURMS Reviewed; 699 AA.
AC A1V1X3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=BMASAVP1_A0886;
OS Burkholderia mallei (strain SAVP1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320388;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAVP1;
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}.
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DR EMBL; CP000526; ABM50068.1; -; Genomic_DNA.
DR RefSeq; WP_011807655.1; NC_008785.1.
DR AlphaFoldDB; A1V1X3; -.
DR KEGG; bmv:BMASAVP1_A0886; -.
DR HOGENOM; CLU_420258_0_0_4; -.
DR OMA; NPEKDWG; -.
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; 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_0000314418"
FT ACT_SITE 311
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ SEQUENCE 699 AA; 71651 MW; 38D057B8BCEC976A CRC64;
MTAIRGGSRR APGLALALLG GVLLGACHGD ENAQVNALPG FVSGSVRKTA YDGASDDLLT
AGLGKTGLGS DTRPGFANPA QPSAAELRCL AIYSNYRALV DITPNGGYGR FWGPNVDLAG
NDTLGEGKIA GTEYLAYSDD GSGRKNVTLL VQVPASFDPA NPCIVTATAS GSRGVYGAIA
AAGEWGLKRG CAVAYNDKGG GNGAHEIGTG VVTLIDGTLA TASSAGSSSL FTASESSSTL
AAFNSAFPNR YAYKHAHSQQ NPEQDWGRVT 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