ID A0A059BKT9_EUCGR Unreviewed; 105 AA.
AC A0A059BKT9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
DE Flags: Fragment;
GN ORFNames=EUGRSUZ_F00257 {ECO:0000313|EMBL:KCW66461.1};
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:KCW66461.1};
RN [1] {ECO:0000313|EMBL:KCW66461.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW66461.1};
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; KCW66461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059BKT9; -.
DR STRING; 71139.A0A059BKT9; -.
DR EnsemblPlants; KCW66461; KCW66461; EUGRSUZ_F00257.
DR Gramene; KCW66461; KCW66461; EUGRSUZ_F00257.
DR InParanoid; A0A059BKT9; -.
DR OMA; VTCMLTA; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1090.10; 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..105
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT NON_TER 105
FT /evidence="ECO:0000313|EMBL:KCW66461.1"
SQ SEQUENCE 105 AA; 11375 MW; FD83ED5C747DF878 CRC64;
MERAMSLPLQ PPTYGNLITI LSIDGGGIRG LIPGTILAFL ESELQKLDGE DARIADYFDV
IAGTSTGGLV TAMLTSPDEN NRPLFAAKDI KDFYLDNCPK IFPQD
//
