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P22088

- LIP_BURCE

UniProt

P22088 - LIP_BURCE

Protein

Lipase

Gene

lipA

Organism
Burkholderia cepacia (Pseudomonas cepacia)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the hydrolysis of triglycerides.

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.

    Cofactori

    Binds 1 calcium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei131 – 1311Nucleophile
    Metal bindingi286 – 2861Calcium
    Active sitei308 – 3081Charge relay system
    Active sitei330 – 3301Charge relay system
    Metal bindingi332 – 3321Calcium
    Metal bindingi336 – 3361Calcium
    Metal bindingi340 – 3401Calcium; via carbonyl oxygen

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. triglyceride lipase activity Source: UniProtKB-EC

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipase (EC:3.1.1.3)
    Alternative name(s):
    Triacylglycerol lipase
    Gene namesi
    Name:lipA
    OrganismiBurkholderia cepacia (Pseudomonas cepacia)
    Taxonomic identifieri292 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 44441 PublicationAdd
    BLAST
    Chaini45 – 364320LipasePRO_0000017740Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi234 ↔ 314

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    364
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni46 – 494
    Beta strandi55 – 584
    Beta strandi61 – 644
    Beta strandi65 – 673
    Turni68 – 703
    Beta strandi71 – 744
    Helixi77 – 837
    Beta strandi88 – 903
    Beta strandi95 – 973
    Beta strandi99 – 1013
    Helixi105 – 12016
    Beta strandi125 – 1306
    Helixi132 – 14312
    Helixi145 – 1473
    Beta strandi148 – 1558
    Helixi162 – 17110
    Helixi178 – 19417
    Helixi204 – 2118
    Helixi213 – 22210
    Beta strandi239 – 2435
    Beta strandi246 – 25510
    Beta strandi258 – 2647
    Beta strandi267 – 2726
    Turni277 – 2793
    Helixi282 – 2854
    Helixi288 – 30013
    Turni301 – 3033
    Beta strandi306 – 3127
    Helixi313 – 3164
    Beta strandi319 – 3268
    Helixi332 – 3343
    Turni335 – 3395
    Helixi348 – 36114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HQDX-ray2.30A45-364[»]
    1OILX-ray2.10A/B45-364[»]
    1YS1X-ray1.10X45-364[»]
    1YS2X-ray1.50X45-364[»]
    2LIPX-ray2.10A45-364[»]
    2NW6X-ray1.80A45-364[»]
    3LIPX-ray2.00A45-364[»]
    4LIPX-ray1.75D/E45-364[»]
    5LIPX-ray2.90A45-364[»]
    ProteinModelPortaliP22088.
    SMRiP22088. Positions 48-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22088.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P22088-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARTMRSRVV AGAVACAMSI APFAGTTAVM TLATTHAAMA ATAPAAGYAA    50
    TRYPIILVHG LSGTDKYAGV LEYWYGIQED LQQNGATVYV ANLSGFQSDD 100
    GPNGRGEQLL AYVKTVLAAT GATKVNLVGH SQGGLSSRYV AAVAPDLVAS 150
    VTTIGTPHRG SEFADFVQDV LAYDPTGLSS SVIAAFVNVF GILTSSSHNT 200
    NQDALAALQT LTTARAATYN QNYPSAGLGA PGSCQTGAPT ETVGGNTHLL 250
    YSWAGTAIQP TLSVFGVTGA TDTSTLPLVD PANVLDLSTL ALFGTGTVMI 300
    NRGSGQNDGL VSKCSALYGK VLSTSYKWNH LDEINQLLGV RGAYAEDPVA 350
    VIRTHANRLK LAGV 364
    Length:364
    Mass (Da):37,494
    Last modified:February 1, 1996 - v2
    Checksum:iE9CD2DBFB55658E9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58494 Genomic DNA. Translation: AAA50466.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58494 Genomic DNA. Translation: AAA50466.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HQD X-ray 2.30 A 45-364 [» ]
    1OIL X-ray 2.10 A/B 45-364 [» ]
    1YS1 X-ray 1.10 X 45-364 [» ]
    1YS2 X-ray 1.50 X 45-364 [» ]
    2LIP X-ray 2.10 A 45-364 [» ]
    2NW6 X-ray 1.80 A 45-364 [» ]
    3LIP X-ray 2.00 A 45-364 [» ]
    4LIP X-ray 1.75 D/E 45-364 [» ]
    5LIP X-ray 2.90 A 45-364 [» ]
    ProteinModelPortali P22088.
    SMRi P22088. Positions 48-364.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P22088.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view ]
    Pfami PF00561. Abhydrolase_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00120. LIPASE_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequence, and expression of a lipase gene from Pseudomonas cepacia: lipase production in heterologous hosts requires two Pseudomonas genes."
      Joergensen S., Skov K.W., Diderichsen B.
      J. Bacteriol. 173:559-567(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 45-66.
      Strain: DSM 3959.
    2. "The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor."
      Kim K.K., Song H.K., Shin D.H., Hwang K.Y., Suh S.W.
      Structure 5:173-185(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    3. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    4. "Structural basis of the chiral selectivity of Pseudomonas cepacia lipase."
      Lang D.A., Mannesse M.L., de Haas G.H., Verheij H.M., Dijkstra B.W.
      Eur. J. Biochem. 254:333-340(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF COMPLEXES WITH 1,2-DIBUTYLCARBAMOYLGLYCERO-3-O-P-NITROPHENYL-BUTYLPHOSPHONATE AND 1,2-DIOCTYLCARBAMOYLGLYCERO-3-O-P-NITROPHENYL-OCTYLPHOSPHONATE INHIBITORS.
      Strain: ATCC 21808 / FERM P-1431 / 156-A.
    5. "Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study."
      Luic M., Tomic S., Lescic I., Ljubovic E., Sepac D., Sunjic V., Vitale L., Saenger W., Kojic-Prodic B.
      Eur. J. Biochem. 268:3964-3973(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH (RP,SP)-O-(2R)-(1-PHENOXYBUT-2-YL)-METHYLPHOSPHONIC ACID CHLORIDE INHIBITOR.

    Entry informationi

    Entry nameiLIP_BURCE
    AccessioniPrimary (citable) accession number: P22088
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3