ID   LIP2_MORS1              Reviewed;         433 AA.
AC   P24484;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Lipase 2;
DE            EC=3.1.1.3;
DE   AltName: Full=Triacylglycerol lipase;
GN   Name=lip2; Synonyms=L2;
OS   Moraxella sp. (strain TA144).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella; unclassified Moraxella.
OX   NCBI_TaxID=77152;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
RX   PubMed=1907455; DOI=10.1089/dna.1991.10.381;
RA   Feller G., Thiry M., Gerday C.;
RT   "Nucleotide sequence of the lipase gene lip2 from the antarctic
RT   psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved
RT   serine and histidine residues.";
RL   DNA Cell Biol. 10:381-388(1991).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Active at temperatures close to 0 degree Celsius.;
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme 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; X53868; CAA37862.1; -; Genomic_DNA.
DR   PIR; A39556; A39556.
DR   AlphaFoldDB; P24484; -.
DR   SMR; P24484; -.
DR   ESTHER; morsp-2lipa; Hormone-sensitive_lipase_like.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
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; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Lipid degradation; Lipid metabolism.
FT   CHAIN           1..433
FT                   /note="Lipase 2"
FT                   /id="PRO_0000071552"
FT   MOTIF           165..167
FT                   /note="Involved in the stabilization of the negatively
FT                   charged intermediate by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        239
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23872,
FT                   ECO:0000255|PROSITE-ProRule:PRU10038"
FT   ACT_SITE        361
FT                   /evidence="ECO:0000250|UniProtKB:P23872"
FT   ACT_SITE        391
FT                   /evidence="ECO:0000250|UniProtKB:P23872"
FT   MUTAGEN         165
FT                   /note="H->Q: Loss of lipase and esterase activity."
FT                   /evidence="ECO:0000269|PubMed:1907455"
FT   MUTAGEN         239
FT                   /note="S->A: Loss of lipase and esterase activity."
FT                   /evidence="ECO:0000269|PubMed:1907455"
SQ   SEQUENCE   433 AA;  47225 MW;  D4E53252BDF12ACD CRC64;
     MPILPVPALN ALLTKTIKTI KTGAAKNAHQ HHVLHHTLKG LDNLPAPVLE RINRRLKAST
     AEQYPLADAH LRLILAISNK LKRPLAIDKL PKLRQKFGTD AVSLQAPSVW QQNADASGST
     ENAVSWQDKT IANADGGDMT VRCYQKSTQN SERKSTDEAA MLFFHGGGFC IGDIDTHHEF
     CHTVCAQTGW AVVSVDYRMA PEYPAPTALK DCLAAYAWLA EHSQSLGASP SRIVLSGDSA
     GGCLAALVAQ QVIKPIDALW QDNNQAPAAD KKVNDTFKNS LADLPRPLAQ LPLYPVTDYE
     AEYPSWELYG EGLLLDHNDA EVFNSAYTQH SGLPQSHPLI SVMHGDNTQL CPSYIVVAEL
     DILRDEGLAY AELLQKEGVQ VQTYTVLGAP HGFINLMSVH QGLGNQTTYI INEFACLVQN
     LLTSEGDKPN LRA