HBOH2_RALPI
ID HBOH2_RALPI Reviewed; 741 AA.
AC Q9X6X9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 50.
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 AltName: Full=Extracellular 3HB-oligomer hydrolase;
DE Short=e3HBOH;
DE Flags: Precursor;
OS Ralstonia pickettii (Burkholderia pickettii).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=329;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T1;
RA Saito T.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=T1;
RX PubMed=15170237; DOI=10.1007/s00284-003-4227-x;
RA Sugiyama A., Kobayashi T., Shiraki M., Saito T.;
RT "Roles of poly(3-hydroxybutyrate) depolymerase and 3HB-oligomer hydrolase
RT in bacterial PHB metabolism.";
RL Curr. Microbiol. 48:424-427(2004).
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 ECO:0000269|PubMed:15170237}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.61 mM for linear 3HB-dimer {ECO:0000269|PubMed:15170237};
CC KM=0.95 mM for linear 3HB-trimer {ECO:0000269|PubMed:15170237};
CC KM=0.86 mM for cyclic 3HB-trimer {ECO:0000269|PubMed:15170237};
CC KM=0.83 mM for linear 3HB-tetramer {ECO:0000269|PubMed:15170237};
CC KM=0.88 mM for linear 3HB-pentamer {ECO:0000269|PubMed:15170237};
CC KM=0.72 mM for cyclic 3HB-pentamer {ECO:0000269|PubMed:15170237};
CC KM=0.62 mM for cyclic 3HB-hexamer {ECO:0000269|PubMed:15170237};
CC Vmax=27 umol/min/mg enzyme with linear 3HB-dimer as substrate
CC {ECO:0000269|PubMed:15170237};
CC Vmax=37 umol/min/mg enzyme with linear 3HB-trimer as substrate
CC {ECO:0000269|PubMed:15170237};
CC Vmax=41 umol/min/mg enzyme with cyclic 3HB-trimer as substrate
CC {ECO:0000269|PubMed:15170237};
CC Vmax=42 umol/min/mg enzyme with linear 3HB-tetramer as substrate
CC {ECO:0000269|PubMed:15170237};
CC Vmax=57 umol/min/mg enzyme with linear 3HB-pentamer as substrate
CC {ECO:0000269|PubMed:15170237};
CC Vmax=41 umol/min/mg enzyme with cyclic 3HB-pentamer as substrate
CC {ECO:0000269|PubMed:15170237};
CC Vmax=42 umol/min/mg enzyme with cyclic 3HB-hexamer as substrate
CC {ECO:0000269|PubMed:15170237};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_01906}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_01906,
CC ECO:0000269|PubMed:15170237}.
CC -!- SIMILARITY: Belongs to the D-(-)-3-hydroxybutyrate oligomer hydrolase
CC family. {ECO:0000255|HAMAP-Rule:MF_01906}.
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DR EMBL; J04223; AAD36989.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9X6X9; -.
DR SABIO-RK; Q9X6X9; -.
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; IPR016582; OHBut_olig_hydro_put.
DR Pfam; PF10605; 3HBOH; 1.
DR PIRSF; PIRSF011409; HObutyrate_olig_hydrol; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT CHAIN 24..741
FT /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT /id="PRO_0000314420"
FT REGION 45..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ SEQUENCE 741 AA; 75590 MW; 68E13C032382B373 CRC64;
MKTIQGKSPG RWYSRGMLLA AMAASGVIGL AACGGGNDGN SAGNNGNAGG NGNNNGNNNG
NTVSNTKPSF VGTVTVRRFD GVSDDLLTAG LGASGLASAT APAVANAVAP TAAELRRLTI
YNNYRALIDT SAKGGYGTLY GPNVDADGNV TSGNGMVAGA EYVAYPDDGS GQQNVVLLVQ
IPDAFDAAHP CIITATSSGS RGIYGAISTG EWGLKRKCAV AYTDKGTGAG PHDLATDTVP
LQDGTRTTRT LAGNTAQFAA PLAASRLAAF NVATPNRLAF KHAHSQRNPE KDWGLFTLQA
VQFAFWAIND KLGISSGQTV SQLPVRPGNT IVIASSVSNG GGAAIAAAEQ DTGNLIDGVA
VGEPALSLPS SINVQVKRGG ASLPINGKPL FDYVSYANEF RLCAALSASV ASAPTQAYFG
AALGWPASVQ ANRCAALHAK GLLSSTTTAA QADEALQKMR DYGWEPESDL LHASMAYFEI
DPSVATTFGN ALARASVFDN LCDLSFAAVD GSFHPATMNA TVLAQLAATG NGVPPTTGVQ
LINNIAQGGA AQSRQSIDSS GTQAANLDGA LCLRNLLSGS DAASQALQLG LSQTLRSGNL
RGKPALIVQG RNDALLPVNH GARPYLGLNA QVDGSSKLSY IEVTNAQHFD GFIDLLPGYD
SLFVPLAVYE QRALDAVYAN LRSGTPLPPS QVVRTTPRGG AAGAAPPITA ANVPNFTMTP
AAGDRIQVSV SGGVATVSVP N
