HBOH_CUPNH
ID HBOH_CUPNH Reviewed; 718 AA.
AC Q0K9H3; O05992;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Intracellular 3HB-oligomer hydrolase;
DE Short=i3HBOH;
GN Name=phaZ2; Synonyms=phaY1; OrderedLocusNames=H16_A2251;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF SER-179; SER-317;
RP SER-320 AND SER-591.
RX PubMed=16233278; DOI=10.1263/jbb.94.106;
RA Saegusa H., Shiraki M., Saito T.;
RT "Cloning of an intracellular D(-)-3-hydroxybutyrate-oligomer hydrolase gene
RT from Ralstonia eutropha H16 and identification of the active site serine
RT residue by site-directed mutagenesis.";
RL J. Biosci. Bioeng. 94:106-112(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, SUBSTRATE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12775684; DOI=10.1128/jb.185.12.3485-3490.2003;
RA Kobayashi T., Shiraki M., Abe T., Sugiyama A., Saito T.;
RT "Purification and properties of an intracellular 3-hydroxybutyrate-oligomer
RT hydrolase (PhaZ2) in Ralstonia eutropha H16 and its identification as a
RT novel intracellular poly(3-hydroxybutyrate) depolymerase.";
RL J. Bacteriol. 185:3485-3490(2003).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
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. Seems to have also poly(3-
CC hydroxybutyrate) depolymerase activity since it is able to release 3HB-
CC monomers from artificial amorphous PHB. {ECO:0000255|HAMAP-
CC Rule:MF_01906, ECO:0000269|PubMed:12775684,
CC ECO:0000269|PubMed:15170237, ECO:0000269|PubMed:16233278}.
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 -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP).
CC {ECO:0000269|PubMed:16233278}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.35 mM for linear 3HB-dimer {ECO:0000269|PubMed:12775684,
CC ECO:0000269|PubMed:15170237};
CC KM=0.33 mM for linear 3HB-trimer {ECO:0000269|PubMed:12775684,
CC ECO:0000269|PubMed:15170237};
CC KM=0.20 mM for cyclic 3HB-trimer {ECO:0000269|PubMed:12775684,
CC ECO:0000269|PubMed:15170237};
CC KM=0.11 mM for linear 3HB-tetramer {ECO:0000269|PubMed:12775684,
CC ECO:0000269|PubMed:15170237};
CC KM=0.15 mM for linear 3HB-pentamer {ECO:0000269|PubMed:12775684,
CC ECO:0000269|PubMed:15170237};
CC KM=0.14 mM for cyclic 3HB-pentamer {ECO:0000269|PubMed:12775684,
CC ECO:0000269|PubMed:15170237};
CC KM=0.25 mM for cyclic 3HB-hexamer {ECO:0000269|PubMed:12775684,
CC ECO:0000269|PubMed:15170237};
CC Vmax=78 umol/min/mg enzyme with linear 3HB-dimer as substrate
CC {ECO:0000269|PubMed:12775684, ECO:0000269|PubMed:15170237};
CC Vmax=59 umol/min/mg enzyme with linear 3HB-trimer as substrate
CC {ECO:0000269|PubMed:12775684, ECO:0000269|PubMed:15170237};
CC Vmax=60 umol/min/mg enzyme with cyclic 3HB-trimer as substrate
CC {ECO:0000269|PubMed:12775684, ECO:0000269|PubMed:15170237};
CC Vmax=54 umol/min/mg enzyme with linear 3HB-tetramer as substrate
CC {ECO:0000269|PubMed:12775684, ECO:0000269|PubMed:15170237};
CC Vmax=50 umol/min/mg enzyme with linear 3HB-pentamer as substrate
CC {ECO:0000269|PubMed:12775684, ECO:0000269|PubMed:15170237};
CC Vmax=59 umol/min/mg enzyme with cyclic 3HB-pentamer as substrate
CC {ECO:0000269|PubMed:12775684, ECO:0000269|PubMed:15170237};
CC Vmax=60 umol/min/mg enzyme with cyclic 3HB-hexamer as substrate
CC {ECO:0000269|PubMed:12775684, ECO:0000269|PubMed:15170237};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_01906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12775684,
CC ECO:0000269|PubMed:16233278}. Note=A fraction is associated with PBH
CC granules.
CC -!- INDUCTION: Induced by PHB accumulation. {ECO:0000269|PubMed:16233278}.
CC -!- SIMILARITY: Belongs to the D-(-)-3-hydroxybutyrate oligomer hydrolase
CC family. {ECO:0000255|HAMAP-Rule:MF_01906}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19964.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB003701; BAA19964.1; ALT_INIT; Genomic_DNA.
DR EMBL; AM260479; CAJ93348.1; -; Genomic_DNA.
DR PIR; T02884; T02884.
DR RefSeq; WP_011615575.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0K9H3; -.
DR STRING; 381666.H16_A2251; -.
DR ESTHER; cupnh-hboh; OHBut_olig_hydro_put.
DR EnsemblBacteria; CAJ93348; CAJ93348; H16_A2251.
DR GeneID; 57644380; -.
DR KEGG; reh:H16_A2251; -.
DR PATRIC; fig|381666.6.peg.2656; -.
DR eggNOG; ENOG502Z8QU; Bacteria.
DR HOGENOM; CLU_420258_0_0_4; -.
DR OMA; NPEKDWG; -.
DR OrthoDB; 865015at2; -.
DR BRENDA; 3.1.1.22; 231.
DR SABIO-RK; Q0K9H3; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..718
FT /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT /id="PRO_0000314429"
FT ACT_SITE 320
FT /note="Charge relay system"
FT MUTAGEN 179
FT /note="S->A: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:16233278"
FT MUTAGEN 317
FT /note="S->A: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:16233278"
FT MUTAGEN 320
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16233278"
FT MUTAGEN 591
FT /note="S->A: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:16233278"
SQ SEQUENCE 718 AA; 74286 MW; 3F0403975A2D22DA CRC64;
MHSTQIPPQQ KQKRRLRLTV LAAAASMLAA ACVSGDDNNN GNGSNPNTKP ANIGTVTINS
YNGTTDDLLT AGLGKDGLAS ATAPLPANPT APTAAELRRY AIHTNYRAIV DTTASGGYGS
LYGPNVDAQG NVTGSDGKVA GVEYLAFSDD GSGQQNVTML VQIPASFNTS KPCMITATSS
GSRGVYGAIA TGEWGLKRGC AVAYTDKGTG AAPHDLDTDT VPLIDGTRAT RAAAGKNAQF
AAPAGATSLA DFTAANPHRL AFKHAHSQRN PEKDWGKFTL QAVEFAIWAI NDRFGAVSAN
GTRQRTLDKD RIVVIASSVS NGGGAAVAAA EQDAGGLIDG VAVGEPNLNM PPNTGIVVQR
GATPVAASGR TLYDYTTTAN LLQHCAARAT ALTQAPFYTN PATATFFANR CQTLAEKGLV
SGANTDEQSA SALQALHDAG WEAESDDLHP SLAVFDVAAA ISVNYANAYA QASVTDRLCG
YSFASTLTDL KPAAIAPAAL ASMFATGNGV PPQPPVQLIN DLDPQHGPYL NLASVSPSTL
REDLNYDGAN CLRSLLAGSD AAARALQAGQ ALTLRNGNLR GKPAVIVHGR SDGLLPVNHT
SRPYLGLNRQ QEGVTSKLSY VEVENAQHFD AFIGLVPGYS NRYVPLHVYL NRALDAVYDN
LTAGKALPPS QVLRTTPRGG TLNTPAPALL PSNVPPFAAS PAAGNAITVN ANAVQVPD
