Reviewed, UniProtKB/Swiss-Prot Q02104 (LIP1_PSYIM)

Names and origin

Protein names

Recommended name:
    Lipase 1
    EC=3.1.1.3
Alternative name(s):
    Triacylglycerol lipase

Gene names

Name:

lip1

Organism

Psychrobacter immobilis

Taxonomic identifier

498 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Psychrobacter

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate.
Subcellular location	Cell outer membrane; Lipid-anchor Potential.
Biophysicochemical properties	Temperature dependence: Active at temperatures close to 0 degree Celsius.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Signal
Molecular function	Hydrolase
PTM	Lipoprotein Palmitate
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell outer membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	triglyceride lipase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 317	299	Lipase 1		PRO_0000017730
Sites
	Active site	74	1	Potential
	Active site	142	1	Charge relay system By similarity
Amino acid modifications
	Lipidation	19	1	N-palmitoyl cysteine Potential
	Lipidation	19	1	S-diacylglycerol cysteine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q02104-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 2ACF344644D54B5C	FASTA	317	35,252
	10 20 30 40 50 60 MLLKRLCFAA LFSLSMVGCT NAPNALAVNT TQKIIQYERN KSDLEIKSLT LASGDKMVYA 70 80 90 100 110 120 ENGNVAGEPL LLIHGFGGNK DNFTRIARQL EGYHLIIPDL LGFGESSKPM SADYRSEAQR 130 140 150 160 170 180 TRLHELLQAK GLASNIHVGG NSMGGAISVA YAAKYPKDVK SLWLVDSAGF WSAGIPKSLE 190 200 210 220 230 240 GATLENNPLL IKSNEDFYKM YDFVMYKPPY LPKSVKAVFA QERIKNKELD AKILEQIVTD 250 260 270 280 290 300 NVEERAKIIA QYKIPTLVVW GDKDQIIKPE TVNLIKKIIP QAQVIMMEDV GHVPMVEALD 310 ETADNYKAFR SILEAQR

References

[1]	"Cloning, sequence and structural features of a lipase from the antarctic facultative psychrophile Psychrobacter immobilis B10." Arpigny J.L., Feller G., Gerday C. Biochim. Biophys. Acta 1171:331-333(1993) [PubMed: 7916627] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: B10.
[2]	Erratum Arpigny J.L., Feller G., Gerday C. Biochim. Biophys. Acta 1263:103-103(1995) [PubMed: 7632728] [Abstract] Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X67712 Genomic DNA. Translation: CAA47949.1.
PIR	S57274. S57275.
3D structure databases
SMR	Q02104. Positions 42-304.
ModBase	Search...
Protein family/group databases
MEROPS	S33.010.
Enzyme and pathway databases
BRENDA	3.1.1.3. 141798.
Family and domain databases
InterPro	IPR000073. AB_hydrolase_1. IPR000639. Epox_hydrolase-like. [Graphical view]
Pfam	PF00561. Abhydrolase_1. 1 hit. [Graphical view]
PRINTS	PR00412. EPOXHYDRLASE.
PROSITE	PS00120. LIPASE_SER. False negative. PS51257. PROKAR_LIPOPROTEIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LIP1_PSYIM

Accession

Primary (citable) accession number: Q02104

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	February 1, 1996
Last modified:	January 19, 2010
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)