ID   PHAZ_PSEOL              Reviewed;         283 AA.
AC   P26495;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Poly(3-hydroxyalkanoate) depolymerase {ECO:0000303|PubMed:1989978};
DE            Short=PHA depolymerase {ECO:0000303|PubMed:1989978};
DE            EC=3.1.1.-;
DE   AltName: Full=ORF2 {ECO:0000303|PubMed:1989978};
DE   AltName: Full=PHB depolymerase;
GN   Name=phaZ {ECO:0000303|PubMed:1476773};
OS   Pseudomonas oleovorans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=GPo1;
RX   PubMed=1989978; DOI=10.1016/s0021-9258(18)52227-4;
RA   Huisman G.W., Wonink E., Meima R., Kazemier B., Terpstra P., Witholt B.;
RT   "Metabolism of poly(3-hydroxyalkanoates) (PHAs) by Pseudomonas oleovorans.
RT   Identification and sequences of genes and function of the encoded proteins
RT   in the synthesis and degradation of PHA.";
RL   J. Biol. Chem. 266:2191-2198(1991).
RN   [2]
RP   GENE NAME.
RX   PubMed=1476773; DOI=10.1111/j.1574-6968.1992.tb05841.x;
RA   Steinbuechel A., Hustede E., Liebergesell M., Pieper U., Timm A.,
RA   Valentin H.;
RT   "Molecular basis for biosynthesis and accumulation of polyhydroxyalkanoic
RT   acids in bacteria.";
RL   FEMS Microbiol. Rev. 9:217-230(1992).
CC   -!- FUNCTION: Complements a mutant that does not degrade PHA; might be a
CC       lipase. {ECO:0000269|PubMed:1989978}.
CC   -!- MISCELLANEOUS: Pseudomonas oleovorans accumulates poly(3-
CC       hydroxyalkanoates) after growth on medium chain length hydrocarbons.
CC       Large amounts of this polyester are synthesized when cells are grown
CC       under nitrogen-limiting conditions. When nitrogen is resupplied in the
CC       medium, the accumulated PHA is degraded. {ECO:0000305|PubMed:1989978}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; M58445; AAA25933.1; -; Genomic_DNA.
DR   PIR; B38604; B38604.
DR   AlphaFoldDB; P26495; -.
DR   SMR; P26495; -.
DR   ESTHER; pseol-phab; PHA_depolymerase_arom.
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; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR011942; PHA_depoly_arom.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR02240; PHA_depoly_arom; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism.
FT   CHAIN           1..283
FT                   /note="Poly(3-hydroxyalkanoate) depolymerase"
FT                   /id="PRO_0000090351"
FT   DOMAIN          30..253
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        102
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
SQ   SEQUENCE   283 AA;  31463 MW;  DBE16F79FC64A9E6 CRC64;
     MPQPYIFRTV ELDNQSIRTA VRPGKPHLTP LLIFNGIGAN LELVFPFIEA LDPDLEVIAF
     DVPGVGGSST PRHPYRFPGL AKLTARMLDY LDYGQVNVIG VSWGGALAQQ FAHDYPERCK
     KLVLAATAAG AVMVPGKPKV LWMMASPRRY VQPSHVIRIA PTIYGGGFRR DPELAMQHAS
     KVRSGGKMGY YWQLFAGLGW TSIHWLHKIQ QPTLVLAGDD DPLIPLINMR LLAWRIPNAQ
     LHIIDDGHLF LITRAEAVAP IIMKFLQQER QRAVMHPRPA SGG