LIP_RHIMI
ID LIP_RHIMI Reviewed; 363 AA.
AC P19515;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Lipase;
DE EC=3.1.1.3;
DE AltName: Full=Triacylglycerol lipase;
DE Flags: Precursor;
OS Rhizomucor miehei.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Rhizomucor.
OX NCBI_TaxID=4839;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3419283; DOI=10.1007/bf02535672;
RA Boel E., Huge-Jensen B., Christensen M., Thim L., Fiil N.P.;
RT "Rhizomucor miehei triglyceride lipase is synthesized as a precursor.";
RL Lipids 23:701-706(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=2304552; DOI=10.1038/343767a0;
RA Brady L., Brzozowski A.M., Derewenda Z.S., Dodson E.J., Dodson G.G.,
RA Tolley S., Turkenburg J.P., Christiansen L., Huge-Jensen B., Norskov L.,
RA Thim L., Menge U.;
RT "A serine protease triad forms the catalytic centre of a triacylglycerol
RT lipase.";
RL Nature 343:767-770(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS).
RX PubMed=2046751; DOI=10.1038/351491a0;
RA Brzozowski A.M., Derewenda U., Derewenda Z.S., Dodson G.G., Lawson D.M.,
RA Turkenburg J.P., Bjorkling F., Huge-Jensen B., Patkar S.A., Thim L.;
RT "A model for interfacial activation in lipases from the structure of a
RT fungal lipase-inhibitor complex.";
RL Nature 351:491-494(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=1737010; DOI=10.1021/bi00120a034;
RA Derewenda U., Brzozowski A.M., Lawson D.M., Derewenda Z.S.;
RT "Catalysis at the interface: the anatomy of a conformational change in a
RT triglyceride lipase.";
RL Biochemistry 31:1532-1541(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SEQUENCE REVISION TO 250.
RX PubMed=1404390; DOI=10.1016/0022-2836(92)90225-9;
RA Derewenda Z.S., Derewenda U., Dodson G.G.;
RT "The crystal and molecular structure of the Rhizomucor miehei
RT triacylglyceride lipase at 1.9-A resolution.";
RL J. Mol. Biol. 227:818-839(1992).
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR PDB; 1TGL; X-ray; 1.90 A; A=95-362.
DR PDB; 3TGL; X-ray; 1.90 A; A=95-363.
DR PDB; 4TGL; X-ray; 2.60 A; A=95-363.
DR PDB; 5TGL; X-ray; 3.00 A; A=95-363.
DR PDB; 6QPP; X-ray; 1.49 A; A=1-363.
DR PDB; 6QPR; X-ray; 1.45 A; A=1-363.
DR PDBsum; 1TGL; -.
DR PDBsum; 3TGL; -.
DR PDBsum; 4TGL; -.
DR PDBsum; 5TGL; -.
DR PDBsum; 6QPP; -.
DR PDBsum; 6QPR; -.
DR AlphaFoldDB; P19515; -.
DR SMR; P19515; -.
DR ESTHER; rhimi-lipas; Lipase_3.
DR BRENDA; 3.1.1.3; 3454.
DR SABIO-RK; P19515; -.
DR EvolutionaryTrace; P19515; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Disulfide bond; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Signal; Zymogen.
FT SIGNAL 1..24
FT PROPEP 25..94
FT /id="PRO_0000017731"
FT CHAIN 95..363
FT /note="Lipase"
FT /id="PRO_0000017732"
FT REGION 33..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:2304552"
FT ACT_SITE 297
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:2304552"
FT ACT_SITE 351
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:2304552"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 123..362
FT /evidence="ECO:0000269|PubMed:1737010"
FT DISULFID 134..137
FT /evidence="ECO:0000269|PubMed:1737010"
FT DISULFID 329..338
FT /evidence="ECO:0000269|PubMed:1737010"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 105..120
FT /evidence="ECO:0007829|PDB:6QPR"
FT TURN 124..129
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:6QPR"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:6QPR"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 203..226
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 239..254
FT /evidence="ECO:0007829|PDB:6QPR"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 276..284
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:6QPR"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:6QPR"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:6QPR"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:6QPR"
SQ SEQUENCE 363 AA; 39602 MW; DAB3C66E024F0E39 CRC64;
MVLKQRANYL GFLIVFFTAF LVEAVPIKRQ SNSTVDSLPP LIPSRTSAPS SSPSTTDPEA
PAMSRNGPLP SDVETKYGMA LNATSYPDSV VQAMSIDGGI RAATSQEINE LTYYTTLSAN
SYCRTVIPGA TWDCIHCDAT EDLKIIKTWS TLIYDTNAMV ARGDSEKTIY IVFRGSSSIR
NWIADLTFVP VSYPPVSGTK VHKGFLDSYG EVQNELVATV LDQFKQYPSY KVAVTGHSLG
GATALLCALD LYQREEGLSS SNLFLYTQGQ PRVGDPAFAN YVVSTGIPYR RTVNERDIVP
HLPPAAFGFL HAGEEYWITD NSPETVQVCT SDLETSDCSN SIVPFTSVLD HLSYFGINTG
LCT
