ID   PHA1_PAULE              Reviewed;         414 AA.
AC   P52090;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Poly(3-hydroxyalkanoate) depolymerase C;
DE            Short=PHA depolymerase;
DE            EC=3.1.1.-;
DE   AltName: Full=PHB depolymerase;
DE   Flags: Precursor;
GN   Name=phaZ1;
OS   Paucimonas lemoignei (Pseudomonas lemoignei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paucimonas.
OX   NCBI_TaxID=29443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8269961; DOI=10.1111/j.1432-1033.1993.tb18424.x;
RA   Jendrossek D., Mueller B., Schlegel G.;
RT   "Cloning and characterization of the poly(hydroxyalkanoic acid)-
RT   depolymerase gene locus, phaZ1, of Pseudomonas lemoignei and its gene
RT   product.";
RL   Eur. J. Biochem. 218:701-710(1993).
CC   -!- FUNCTION: Specific for poly(hydroxyalkanoic acid) consisting of
CC       monomers of four or five carbon atoms and for P-nitrophenylbutyrate as
CC       substrates.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z22595; CAA80310.1; -; Genomic_DNA.
DR   PIR; S39530; S39530.
DR   AlphaFoldDB; P52090; -.
DR   SMR; P52090; -.
DR   ESTHER; psele-pha1; Esterase_phb.
DR   BRENDA; 3.1.1.75; 5133.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR010126; Esterase_phb.
DR   Pfam; PF10503; Esterase_PHB; 1.
DR   SUPFAM; SSF53474; SSF53474; 2.
DR   TIGRFAMs; TIGR01840; esterase_phb; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Secreted; Signal.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..414
FT                   /note="Poly(3-hydroxyalkanoate) depolymerase C"
FT                   /id="PRO_0000017728"
FT   ACT_SITE        154
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   414 AA;  43496 MW;  C1F7CDCFC59FB111 CRC64;
     MLAKQIKKAN SRSTLLRKSL LFAAPIILAV SSSSVYALTQ VSNFGTNPGN LQMFKHVPSG
     MPANAPLVVA LHGCTQTAAA YEASGWSALG NTHKFYVVYP QQQSGNNSNK CFNWFEPGDI
     TRGQGEALSI KQMVDNMKAN HSIDPSRVYV TGLSAGAFMT TVMAATYPDV FAGAAPIAGG
     PYKCATSMTS AFTCMSPGVD KTPAAWGDLA RGGYSGYNGP KPKISIWHGS SDYTVAPANQ
     NETVEQFTNY HGIDQTPDVS DTVGGFPHKV YKSANGTPLV ETYTITGMGH GTPVDPGTGA
     NQCGTAGAYI LDVNVCSSYY IGQFFGIIGG GGTTTTTTSG NVTTTTAATT TTTTATQGYT
     QTTSATVTNH YVAGRINVTQ YNVLGARYGY VTTIPLYYCP SLSGWTDKAN CSPI