This family corresponds to family I.3 of the classification of Arpigny and Jaeger (1999) The N-catalytic domain (residues 1-370) contains the active site residues, Ser207, Asp255, and His313 4, 5. The C-domain contains several repeats of the RTX motif and a putative secretion signal near the C-terminus. The C-domain contains two beta-roll motifs, laterally stacked together forming the so called beta-roll sandwich. The first beta-roll motif consists of residues 373-417, containing five RTX repeats and binds three Ca2+ ions. The second beta-roll motif consists of residues 493-568, containing eight RTX repeats and binds five Ca2+ ions. HemolysinCabind (PF00353). This family contains Polyurethanases (PURase)
Interpro : No interpro
PIRSF : No PIRSF
Pdoc : No Pdoc
Pfam : No Pfam
Prints : No Print
EC Number : No EC Number
Peptide in | Fasta |
Nucleotide in | Fasta |
Alignment with Multalin | Text only |
Seed alignment with MAFFT | No colour / coloured with Mview |
Alignment with MAFFT | No colour / coloured with Mview |
Dendrogram | The dnd file |
Structure | Name | Proteins |
---|---|---|
2ZVD | Crystal structure of Pseudomonas sp. MIS38 lipase in an open conformation | psesp-Q9RBY1 |
2ZJ6 | Crystal structure of D337A mutant of Pseudomonas sp. MIS38 lipase | psesp-Q9RBY1 |
2ZJ7 | Crystal structure of D157A mutant of Pseudomonas sp. MIS38 lipase | psesp-Q9RBY1 |
3A6Z | Crystal structure of Pseudomonas sp. MIS38 lipase (PML) in the open conformation following dialysis against Ca-free buffer | psesp-Q9RBY1 |
3A70 | Crystal structure of Pseudomonas sp. MIS38 lipase in complex with diethyl phosphate | psesp-Q9RBY1 |
2Z8X | Crystal structure of extracellular lipase from Pseudomonas sp. MIS38 (CASP Target) | psesp-Q9RBY1 |
2Z8Z | Crystal structure of a platinum-bound S445C mutant of Pseudomonas sp. MIS38 lipase | psesp-Q9RBY1 |
2QUA | Crystal structure of extracellular lipase LipA from Serratia marcescens Space Group P321 | serma-lipasA |
2QUB | Crystal structure of extracellular lipase LipA from Serratia marcescens Space Group H3 | serma-lipasA |
Gene_locus | Name | Species |
---|---|---|
9sped-a0a0s2cee2 | Candidatus Pseudomonas adelgestsugas\; Pseudomonas sp. strain TB11 esterase | Candidatus Pseudomonas adelgestsugas |
psefs-c3kbe9 | Pseudomonas fluorescens (strain SBW25)lipB Thermostable and Organic Solution-Tolerant Lipase | Pseudomonas fluorescens SBW25 |
9bact-g9hwf0 | uncultured bacterium Lipase lipB SMlipB | uncultured bacterium |
psesp-PURase | Pseudomonas sp Polyurethanase (PURase) | Pseudomonas sp. |
serli-a0a109z2v1 | Serratia liquefaciens polyurethanase | Serratia liquefaciens |
9psed-LipYY31 | Pseudomonas sp. strain YY31 solvent-tolerant lipase from a psychrotrophic bacterium | Pseudomonas sp. YY31 |
9bact-q6xci1 | uncultured bacterium lipb | uncultured bacterium |
9bact-q6xci2 | uncultured bacterium lipa | uncultured bacterium |
9psed-q2ktb3 | Pseudomonas sp. 7323 cold-active lipase (EC 3.1.1.3) | Pseudomonas sp. 7323 |
9psed-q6vef5 | Pseudomonas sp. JZ-2003 lipase | Pseudomonas sp. JZ-2003 |
9psed-q66wt1 | uncultured Pseudomonas sp lipase lipJ03 | uncultured Pseudomonas sp. |
pholl-q7n4l7 | Photorhabdus luminescens (subsp. laumondii) similar to lipase | Photorhabdus luminescens |
psebr-lipa | Pseudomonas brassicacearum lipa | Pseudomonas brassicacearum |
psech-PUEA | Pseudomonas chlororaphis (Pseudomonas aureofaciens) polyurethanase esterase a PUEA | Pseudomonas chlororaphis |
psech-PUEB | Pseudomonas chlororaphis (Pseudomonas aureofaciens) polyurethanase esterase b PUEB | Pseudomonas chlororaphis |
psef5-q4kbs3 | Pseudomonas protegens (strain Pf-5 \/ ATCC BAA-477) polyurethanase B PUEB and secreted hemolysin-type EhxA RTX family calcium-binding bacteriocin, putative | Pseudomonas fluorescens |
psef5-q4kbs6 | Pseudomonas protegens (strain Pf-5 \/ ATCC BAA-477) polyurethanase A PUEA and secreted hemolysin-type RTX family calcium-binding bacteriocin | Pseudomonas fluorescens |
psefl-LIPAPF33 | Pseudomonas fluorescens\; Pseudomonas sp. AMS8 lipase LipAMS8, extracellular lipase | Pseudomonas fluorescens |
psefl-lipb | Pseudomonas fluorescens lipase | Pseudomonas fluorescens |
psefl-LIPB2 | Pseudomonas fluorescens lipase | Pseudomonas fluorescens |
psefl-PULA | Pseudomonas fluorescens polyurethanase lipase A | Pseudomonas fluorescens |
psefl-q6gx93 | Pseudomonas fluorescens ( and strain PfO-1) lipase | Pseudomonas fluorescens |
psefl-q7wzt7 | Pseudomonas fluorescens lipase lipJ02 | Pseudomonas fluorescens |
psefl-q76d31 | Pseudomonas fluorescens lipase (EC 3.1.1.3) | Pseudomonas fluorescens |
psefl-q670w0 | Pseudomonas fluorescens lipase | Pseudomonas fluorescens |
psefl-siklip | Pseudomonas fluorescens gene for triacylglycerol lipase, complete cds | Pseudomonas fluorescens |
psefl-TLIA | Pseudomonas fluorescens thermostable lipase tlia | Pseudomonas fluorescens |
psepf-q3kcs9 | Pseudomonas fluorescens (strain PfO-1) triacylglycerol lipase (EC 3.1.1.3) | Pseudomonas fluorescens |
psesp-KBLIP | Pseudomonas sp. KB700A lipase | Pseudomonas sp. KB700A |
psesp-LIPUB48 | Pseudomonas sp. UB48 lipase | Pseudomonas sp. UB48 |
psesp-Q9RBY1 | ![]() |
Pseudomonas sp. MIS38 |
psesp-Q52515 | Pseudomonas sp lipase | Pseudomonas sp. |
serma-lipasA | ![]() |
Serratia marcescens |
psywf-a5wgv1 | Psychrobacter sp. (strain PRwf-1) Triacylglycerol lipase | Psychrobacter sp. PRwf-1 |
Inhibitor | Chemical Nomenclature | Proteins |
---|---|---|
Paraoxon | diethyl (4-nitrophenyl) phosphate | human-PLA2G7 human-PNLIPRP2 humin-cut human-ACHE promi-c2lfd0 yeast-yjg8 bacpu-AXE sulto-ST0071 aspor-cutas pig-1plip fusso-cutas lacrh-B2CZF3 thema-TM0033 colgl-cutas psesp-Q9RBY1 actde-CXE1 myctu-a85c thema-TM0077 rhimi-lipas bacpu-w8fke7 9bact-KP212148 |
Title : Enhanced enzyme thermostability of a family I.3 lipase LipSR1 by T118A mutation at the calcium-binding site - Jiang_2023_Biotechnol.Lett__ |
Author(s) : Jiang S , Zhou Z , Han J , Fan Q , Long Z , Wang J |
Ref : Biotechnol Lett , : , 2023 |
Abstract : |
PubMedSearch : Jiang_2023_Biotechnol.Lett__ |
PubMedID: 37439931 |
Gene_locus related to this paper: lacac-q5fi30 |
Title : X-ray crystallographic and MD simulation studies on the mechanism of interfacial activation of a family I.3 lipase with two lids - Angkawidjaja_2010_J.Mol.Biol_400_82 |
Author(s) : Angkawidjaja C , Matsumura H , Koga Y , Takano K , Kanaya S |
Ref : Journal of Molecular Biology , 400 :82 , 2010 |
Abstract : |
PubMedSearch : Angkawidjaja_2010_J.Mol.Biol_400_82 |
PubMedID: 20438738 |
Gene_locus related to this paper: psesp-Q9RBY1 |
Title : Importance of the Ca2+-binding sites in the N-catalytic domain of a family I.3 lipase for activity and stability - Kuwahara_2008_Protein.Eng.Des.Sel_21_737 |
Author(s) : Kuwahara K , Angkawidjaja C , Matsumura H , Koga Y , Takano K , Kanaya S |
Ref : Protein Engineering Des Sel , 21 :737 , 2008 |
Abstract : |
PubMedSearch : Kuwahara_2008_Protein.Eng.Des.Sel_21_737 |
PubMedID: 18987131 |
Gene_locus related to this paper: psesp-Q9RBY1 |
Title : A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens - Meier_2007_J.Biol.Chem_282_31477 |
Author(s) : Meier R , Drepper T , Svensson V , Jaeger KE , Baumann U |
Ref : Journal of Biological Chemistry , 282 :31477 , 2007 |
Abstract : |
PubMedSearch : Meier_2007_J.Biol.Chem_282_31477 |
PubMedID: 17728256 |
Gene_locus related to this paper: serma-lipasA |
Title : Crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conformation - Angkawidjaja_2007_FEBS.Lett_581_5060 |
Author(s) : Angkawidjaja C , You DJ , Matsumura H , Kuwahara K , Koga Y , Takano K , Kanaya S |
Ref : FEBS Letters , 581 :5060 , 2007 |
Abstract : |
PubMedSearch : Angkawidjaja_2007_FEBS.Lett_581_5060 |
PubMedID: 17923123 |
Gene_locus related to this paper: psesp-Q9RBY1 |
Title : Lipases for biotechnology - Jaeger_2002_Curr.Opin.Biotechnol_13_390 |
Author(s) : Jaeger KE , Eggert T |
Ref : Curr Opin Biotechnol , 13 :390 , 2002 |
Abstract : |
PubMedSearch : Jaeger_2002_Curr.Opin.Biotechnol_13_390 |
PubMedID: 12323363 |
Title : Bacterial lipolytic enzymes: classification and properties - Arpigny_1999_Biochem.J_343_177 |
Author(s) : Arpigny JL , Jaeger KE |
Ref : Biochemical Journal , 343 :177 , 1999 |
Abstract : |
PubMedSearch : Arpigny_1999_Biochem.J_343_177 |
PubMedID: 10493927 |