ID   A0A059BK59_EUCGR        Unreviewed;       423 AA.
AC   A0A059BK59;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN   ORFNames=EUGRSUZ_F00254 {ECO:0000313|EMBL:KCW66458.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW66458.1};
RN   [1] {ECO:0000313|EMBL:KCW66458.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW66458.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lipolytic acyl hydrolase (LAH).
CC       {ECO:0000256|RuleBase:RU361262}.
CC   -!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
CC       motif define the oxyanion hole, and stabilize the oxyanion that forms
CC       during the nucleophilic attack by the catalytic serine during substrate
CC       cleavage. {ECO:0000256|RuleBase:RU361262}.
CC   -!- SIMILARITY: Belongs to the patatin family.
CC       {ECO:0000256|ARBA:ARBA00010240, ECO:0000256|RuleBase:RU361262}.
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DR   EMBL; KK198758; KCW66458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059BK59; -.
DR   EnsemblPlants; KCW66458; KCW66458; EUGRSUZ_F00254.
DR   Gramene; KCW66458; KCW66458; EUGRSUZ_F00254.
DR   eggNOG; KOG0513; Eukaryota.
DR   InParanoid; A0A059BK59; -.
DR   OMA; VICEDRS; -.
DR   GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR   GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07214; Pat17_isozyme_like; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   PANTHER; PTHR32176:SF103; OS08G0376550 PROTEIN; 1.
DR   PANTHER; PTHR32176; XYLOSE ISOMERASE; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU361262};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU361262};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU361262}.
FT   DOMAIN          21..227
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          395..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   423 AA;  46425 MW;  F6D5A1DB14012D74 CRC64;
     MERTTSLPLQ PPTYGNLITI LSIDGGGIRG LIPGTILDFL ESELQKLDGE DARIADYFDV
     IAGTSTGGLV TAMLTTPDDN NRPLFAAKDI KNFYLDNCPK IFPQDSCPFA PATKMIKAVT
     GPKYDGKYLH NLVKEKLGNA RLHQTLTNVV IPTFDIKRLQ PTIFSSYEVK KTPTLDALLS
     DICISTSAAP TYLPAHYFET QDSKRKLREF NLIDGGVAAN NPTLVAMGEV TKEIMGGSSD
     FFPIKPMDYR RFLVISLGTG SRNSEGKYDA SEAAKWGVLN WLTCNGGSPL IDVFMQASAD
     MVDFHLSAVF QALHLEANYL RIQDDNLSGA VASVDIATKK NLNDLVRTGE ALLKKPVSKV
     DLEKGGCEAC NPETNEEALR RFAKMLSNER QLRLARSPHG HNSANLKRSN LSSQQTVICE
     DRS
//