ID   PHB_RALPI               Reviewed;         488 AA.
AC   P12625;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Poly(3-hydroxybutyrate) depolymerase;
DE            Short=PHB depolymerase;
DE            EC=3.1.1.75;
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;
RX   PubMed=2644188; DOI=10.1128/jb.171.1.184-189.1989;
RA   Saito T., Suzuki K., Yamamoto J., Fukui T., Miwa K., Tomita K.,
RA   Nakanishi S., Odani S., Suzuki J., Ishikawa K.;
RT   "Cloning, nucleotide sequence, and expression in Escherichia coli of the
RT   gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis.";
RL   J. Bacteriol. 171:184-189(1989).
RN   [2]
RP   DOMAIN FIBRONECTIN TYPE-III.
RX   PubMed=1409594; DOI=10.1073/pnas.89.19.8990;
RA   Bork P., Doolittle R.F.;
RT   "Proposed acquisition of an animal protein domain by bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8990-8994(1992).
CC   -!- FUNCTION: This protein degrades water-insoluble and water-soluble PHB
CC       to monomeric D(-)-3-hydroxybutyrate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(3R)-hydroxybutanoate](n) + H2O = (3R)-hydroxybutanoate dimer
CC         + [(3R)-hydroxybutanoate](n-2) + H(+); Xref=Rhea:RHEA:56392,
CC         Rhea:RHEA-COMP:14464, Rhea:RHEA-COMP:14519, ChEBI:CHEBI:8298,
CC         ChEBI:CHEBI:10979, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378; EC=3.1.1.75;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(3R)-hydroxybutanoate](n) + H2O = (3R)-hydroxybutanoate
CC         trimer + [(3R)-hydroxybutanoate](n-3) + H(+); Xref=Rhea:RHEA:56396,
CC         Rhea:RHEA-COMP:14464, Rhea:RHEA-COMP:14520, ChEBI:CHEBI:8298,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:140385;
CC         EC=3.1.1.75;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(3R)-hydroxybutanoate](n) + H2O = (R)-3-hydroxybutanoate +
CC         [(3R)-hydroxybutanoate](n-1) + H(+); Xref=Rhea:RHEA:11248, Rhea:RHEA-
CC         COMP:14464, Rhea:RHEA-COMP:14518, ChEBI:CHEBI:8298,
CC         ChEBI:CHEBI:10983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378; EC=3.1.1.75;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(3R)-hydroxybutanoate](n) + H2O = (3R)-hydroxybutanoate
CC         pentamer + [(3R)-hydroxybutanoate](n-5) + H(+); Xref=Rhea:RHEA:56404,
CC         Rhea:RHEA-COMP:14464, Rhea:RHEA-COMP:14522, ChEBI:CHEBI:8298,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:140383;
CC         EC=3.1.1.75;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(3R)-hydroxybutanoate](n) + H2O = (3R)-hydroxybutanoate
CC         tetramer + [(3R)-hydroxybutanoate](n-4) + H(+); Xref=Rhea:RHEA:56400,
CC         Rhea:RHEA-COMP:14464, Rhea:RHEA-COMP:14521, ChEBI:CHEBI:8298,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:140384;
CC         EC=3.1.1.75;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; J04223; AAA21974.1; -; Genomic_DNA.
DR   PIR; A32235; A32235.
DR   AlphaFoldDB; P12625; -.
DR   SMR; P12625; -.
DR   ESTHER; alcfa-phb; Esterase_phb.
DR   BRENDA; 3.1.1.75; 5160.
DR   SABIO-RK; P12625; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050526; F:poly(3-hydroxybutyrate) depolymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR010126; Esterase_phb.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF10503; Esterase_PHB; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF53474; SSF53474; 2.
DR   TIGRFAMs; TIGR01840; esterase_phb; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Secreted; Signal.
FT   SIGNAL          1..27
FT   CHAIN           28..488
FT                   /note="Poly(3-hydroxybutyrate) depolymerase"
FT                   /id="PRO_0000017727"
FT   DOMAIN          346..428
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   ACT_SITE        166
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   488 AA;  49935 MW;  FE6E2BCA97C135EF CRC64;
     MVRRLWRRIA GWLAACVAIL CAFPLHAATA GPGAWSSQQT WAADSVNGGN LTGYFYWPAS
     QPTTPNGKRA LVLVLHGCVQ TASGDVIDNA NGAGFNWKSV ADQYGAVILA PNATGNVYSN
     HCWDYANASP SRTAGHVGVL LDLVNRFVTN SQYAIDPNQV YVAGLSSGGG MTMVLGCIAP
     DIFAGIGINA GPPPGTTTAQ IGYVPSGFTA TTAANKCNAW AGSNAGKFST QIAGAVWGTS
     DYTVAQAYGP MDAAAMRLVY GGNFTQGSQV SISGGGTNTP YTDSNGKVRT HEISVSGMAH
     AWPAGTGGDN TNYVDATHIN YPVFVMDYWV KNNLRAGSGT GQAGSAPTGL AVTATTSTSV
     SLSWNAVANA SSYGVYRNGS KVGSATATAY TDSGLIAGTT YSYTVTAVDP TAGESQPSAA
     VSATTKSAFT CTATTASNYA HVQAGRAHDS GGIAYANGSN QSMGLDNLFY TSTLAQTAAG
     YYIVGNCP