Reviewed, UniProtKB/Swiss-Prot P24484 (LIP2_MORS1)

Names and origin

Protein names

Recommended name:
    Lipase 2
    EC=3.1.1.3
Alternative name(s):
    Triacylglycerol lipase

Gene names

Name:	lip2
Synonyms:	L2

Organism

Moraxella sp. (strain TA144)

Taxonomic identifier

77152 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Moraxella

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate.
Sequence similarities	Belongs to the 'GDXG' lipolytic enzyme family.
Biophysicochemical properties	Temperature dependence: Active at temperatures close to 0 degree Celsius.

Ontologies

Keywords
Biological process	Lipid degradation
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	lipid catabolic process 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
	Chain	1 – 433	433	Lipase 2		PRO_0000071552
Sites
	Active site	165	1	Potential
	Active site	239	1	Charge relay system By similarity
Experimental info
	Mutagenesis	165	1	H → Q: Loss of lipase and esterase activity.
	Mutagenesis	239	1	S → A: Loss of lipase and esterase activity.

Sequences

	Sequence		Length	Mass (Da)
	P24484-1 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: D4E53252BDF12ACD	FASTA	433	47,225
	10 20 30 40 50 60 MPILPVPALN ALLTKTIKTI KTGAAKNAHQ HHVLHHTLKG LDNLPAPVLE RINRRLKAST 70 80 90 100 110 120 AEQYPLADAH LRLILAISNK LKRPLAIDKL PKLRQKFGTD AVSLQAPSVW QQNADASGST 130 140 150 160 170 180 ENAVSWQDKT IANADGGDMT VRCYQKSTQN SERKSTDEAA MLFFHGGGFC IGDIDTHHEF 190 200 210 220 230 240 CHTVCAQTGW AVVSVDYRMA PEYPAPTALK DCLAAYAWLA EHSQSLGASP SRIVLSGDSA 250 260 270 280 290 300 GGCLAALVAQ QVIKPIDALW QDNNQAPAAD KKVNDTFKNS LADLPRPLAQ LPLYPVTDYE 310 320 330 340 350 360 AEYPSWELYG EGLLLDHNDA EVFNSAYTQH SGLPQSHPLI SVMHGDNTQL CPSYIVVAEL 370 380 390 400 410 420 DILRDEGLAY AELLQKEGVQ VQTYTVLGAP HGFINLMSVH QGLGNQTTYI INEFACLVQN 430 LLTSEGDKPN LRA

References

[1]

"Nucleotide sequence of the lipase gene lip2 from the antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues." Feller G., Thiry M., Gerday C. DNA Cell Biol. 10:381-388(1991) [PubMed: 1907455] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X53868 Genomic DNA. Translation: CAA37862.1.
PIR	A39556.
3D structure databases
SMR	P24484. Positions 121-398.
ModBase	Search...
Family and domain databases
InterPro	IPR002168. Lipase_GDXG_AS. [Graphical view]
PROSITE	PS01173. LIPASE_GDXG_HIS. 1 hit. PS01174. LIPASE_GDXG_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LIP2_MORS1

Accession

Primary (citable) accession number: P24484

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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