HBOH_POLSJ
ID HBOH_POLSJ Reviewed; 706 AA.
AC Q122D1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=Bpro_4732;
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500;
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE46611.1; -; Genomic_DNA.
DR RefSeq; WP_011485596.1; NC_007948.1.
DR AlphaFoldDB; Q122D1; -.
DR STRING; 296591.Bpro_4732; -.
DR ESTHER; polsj-hboh; OHBut_olig_hydro_put.
DR EnsemblBacteria; ABE46611; ABE46611; Bpro_4732.
DR KEGG; pol:Bpro_4732; -.
DR eggNOG; ENOG502Z8QU; Bacteria.
DR HOGENOM; CLU_420258_0_0_4; -.
DR OMA; NPEKDWG; -.
DR OrthoDB; 865015at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000001983; 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..32
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT CHAIN 33..706
FT /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT /id="PRO_5000117312"
FT ACT_SITE 311
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ SEQUENCE 706 AA; 72212 MW; 92792A8B4905943B CRC64;
MTTTSKNCLT LTSIAAAVAA VLVLSACGGG SAGENINRKP TYLGTVVSVN YDGASDDLLT
AGLGKTGLGA TAPVAADPLN PTAAELRRIA IFNNYRALLD ISVAGGYGSL YGPNVDASGV
ITTSEGKIAG TEYMAYSDDG TGNQNITMLV QVPTTFNPAS PCIVTGTSSG SRGVYGAIGT
SGEWGLKNGC AVAYTDKGTG TGIHDLQNDT VNLQRGERAT ATAAGKASNF TASLTSTERA
AFNTATPNRF AVKHAHSQQN TEKDWGKWTL QAVEFAYFVL NENYGDAAKD GVSRLVKLKP
ANTIVIASSA SNGAGAALAA AELDTKGLIT GVAVAEPQIQ VVPDTRLSVR RGASTLGGTG
RSLFDYASLG NLLQPCAALA SPTTNVFNTV NTTIATNRCN ALQASGLIVG NTTAELAADA
MARLLAAGHQ PESSVLQASH YSFATPAVAV TFANSYGRFS VKDNLCGFSF AATGAAGSAT
PNAPVAASAA ALATSFGASN GIPPTVGINI VNNNSVGGPL LDAASLSAGS VLDYNIAGAL
CLRELLGGSS ANALKVQQGI NEVLRTGDLQ GKPALIVHGR ADAQVPVAFS SRPYFGRNKI
VEGANSRLSY IEVTNAQHFD AFLAFPGYGE RFVPAHRYFI QAMDMMYANL KTGAALPASQ
VVRTVPRGLT GAVVNPITPA NVPPIKTVPA VADQITFANN VVTVAD