Lipase - Geobacillus stearothermophilus

Preferred order of sections

Names and origin

Protein names	Submitted name: Lipase EMBL AAC12257.1 EC=3.1.1.3 EMBL AAC12257.1
Organism	Geobacillus stearothermophilus (Bacillus stearothermophilus) EMBL AAC12257.1
Taxonomic identifier	1422 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 1KU0 Metal-binding PDB 1KU0 Zinc PDB 1KU0
Molecular function	Hydrolase EMBL AAC12257.1
Technical term	3D-structure PDB 1KU0
Gene Ontology (GO)
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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

Sites

Metal binding

90

1

Zinc PDB 1KU0

Metal binding

110

1

Zinc; via tele nitrogen PDB 1KU0

Metal binding

116

1

Zinc; via tele nitrogen PDB 1KU0

Metal binding

267

1

Zinc PDB 1KU0

Metal binding

315

1

Calcium; via carbonyl oxygen PDB 1KU0

Metal binding

389

1

Calcium PDB 1KU0

Metal binding

394

1

Calcium PDB 1KU0

Metal binding

395

1

Calcium; via carbonyl oxygen PDB 1KU0

Sequences

Sequence

Length

Mass (Da)

Tools

O66015 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: E2576FFD658EBCE5
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FASTA

417

46,257

        10         20         30         40         50         60 
MMKGCRVMVV LLGLWFVFGL SVPGGRTEAA SPRANDAPIV LLHGFTGWGR EEMLGFKYWG 

        70         80         90        100        110        120 
GVRGDIEQWL NDNGYRTYTL AVGPLSSNWD RACEAYAQLV GGTVDYGAAH AANDGHARFG 

       130        140        150        160        170        180 
RTYPGLLPEL KRGGRVHIIA HSQGGQTARM LVSLLENGSQ EEREYAKEHN VSLSPLFEGG 

       190        200        210        220        230        240 
HRFVLSVTTI ATPHDGTTLV NMVDFTDRFF DLQKAVLEAA AVASNAPYTS EIYDFKLDQW 

       250        260        270        280        290        300 
GLRREPGESF DHYFERLKRS PVWTSTDTAR YDLSVPGAET LNRWVKASPN TYYLSFSTER 

       310        320        330        340        350        360 
TYRGALTGNY YPELGMNAFS AIVCAPFLGS YRNAALGIDS HWLGNDGIVN TISMNGPKRG 

       370        380        390        400        410 
SNDRIVPYDG TLKKGVWNDM GTYKVDHLEV IGVDPNPSFN IRAFYLRLAE QLASLRP

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References

[1]	"Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1." Kim H.K., Park S.Y., Lee J.K., Oh T.K. Biosci. Biotechnol. Biochem. 62:66-71(1998) [PubMed: 9501519] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: L1 EMBL AAC12257.1.
[2]	"Novel zinc-binding center and a temperature switch in the Bacillus stearothermophilus L1 lipase." Jeong S.T., Kim H.K., Kim S.J., Chi S.W., Pan J.G., Oh T.K., Ryu S.E. J. Biol. Chem. 277:17041-17047(2002) [PubMed: 11859083] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 30-417 IN COMPLEX WITH CALCIUM AND ZINC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U78785 Genomic DNA. Translation: AAC12257.1.

PIR

JW0068.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KU0	X-ray	2.00	A/B	30-417	[»]

ProteinModelPortal

O66015.

SMR

O66015. Positions 30-417.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

ProtoNet

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Entry information

Entry name

O66015_GEOSE

Accession

Primary (citable) accession number: O66015

Entry history

Integrated into UniProtKB/TrEMBL:	August 1, 1998
Last sequence update:	August 1, 1998
Last modified:	February 8, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)