ID LIP3_MORS1 Reviewed; 315 AA.
AC P24640;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-MAY-2023, entry version 84.
DE RecName: Full=Lipase 3;
DE EC=3.1.1.3;
DE AltName: Full=Triacylglycerol lipase;
DE Flags: Precursor;
GN Name=lip3; Synonyms=L3;
OS Moraxella sp. (strain TA144).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=77152;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2001407; DOI=10.1016/0167-4781(91)90073-u;
RA Feller G., Thiry M., Gerday C.;
RT "Nucleotide sequence of the lipase gene lip3 from the antarctic psychotroph
RT Moraxella TA144.";
RL Biochim. Biophys. Acta 1088:323-324(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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO family.
CC {ECO:0000305}.
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DR EMBL; X53869; CAA37863.1; -; Genomic_DNA.
DR PIR; S14276; S14276.
DR AlphaFoldDB; P24640; -.
DR SMR; P24640; -.
DR ESTHER; morsp-3lipa; ABHD6-Lip.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR PANTHER; PTHR43798:SF5; MONOACYLGLYCEROL LIPASE ABHD6; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Lipid degradation; Lipid metabolism; Lipoprotein;
KW Membrane; Palmitate; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..315
FT /note="Lipase 3"
FT /id="PRO_0000008547"
FT DOMAIN 69..296
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 74
FT /evidence="ECO:0000255"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 315 AA; 34774 MW; 9007D9741EE04DFB CRC64;
MLLKRLGLAA LFSLSMVGCT TAPNTLAVNT TQKIIQYERS KSDLEVKSLT LASGDKMVYA
ENDNVTGEPL LLIHGFGGNK DNFTRIADKL EGYHLIIPDL LGFGNSSKPM TADYRADAQA
TRLHELMQAK GLASNTHVGG NSMGGAISVA YAAKYPKEIK SLWLVDTAGF WSAGVPKSLE
GATLENNPLL INSKEDFYKM YDFVMYKPPY IPKSVKAVFA QERINNKALD TKILEQIVTD
NVEERAKIIA KYNIPTLVVW GDKDQVIKPE TTELIKEIIP QAQVIMMNDV GHVPMVEAVK
DTANDYKAFR DGLKK
//
