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Protein

Carboxylesterase

Gene

est

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the detoxification of xenobiotics. Shows maximal activity with C6 substrates, with gradually decreasing activity from C8 to C12 substrates. No activity for higher chain length substrates acids rather than long-chain ones.

Catalytic activityi

A carboxylic ester + H2O = an alcohol + a carboxylate.1 Publication

Kineticsi

  1. KM=2.16 µM for p-nitrophenyl caproate (at 60 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 9.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei93 – 931Nucleophile
    Active sitei192 – 1921Charge relay system
    Active sitei222 – 2221Charge relay system

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Enzyme and pathway databases

    BRENDAi3.1.1.1. 623.
    SABIO-RKQ06174.

    Protein family/group databases

    ESTHERigeost-est30. CarbLipBact_1.
    MEROPSiS09.946.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxylesterase (EC:3.1.1.1)
    Gene namesi
    Name:est
    Synonyms:est30
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 246246CarboxylesterasePRO_0000008548Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    246
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 113Combined sources
    Beta strandi17 – 215Combined sources
    Helixi29 – 4012Combined sources
    Beta strandi44 – 474Combined sources
    Beta strandi53 – 553Combined sources
    Helixi57 – 604Combined sources
    Helixi65 – 8117Combined sources
    Beta strandi87 – 926Combined sources
    Helixi94 – 10310Combined sources
    Beta strandi111 – 1155Combined sources
    Helixi123 – 14119Combined sources
    Helixi145 – 15511Combined sources
    Helixi163 – 17513Combined sources
    Helixi176 – 1794Combined sources
    Beta strandi184 – 1896Combined sources
    Beta strandi193 – 1953Combined sources
    Helixi199 – 2068Combined sources
    Beta strandi210 – 2178Combined sources
    Helixi224 – 2263Combined sources
    Helixi230 – 24314Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R1DX-ray2.00A/B1-246[»]
    1TQHX-ray1.63A1-246[»]
    ProteinModelPortaliQ06174.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06174.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the lipase/esterase LIP3/BchO family.Curated

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR012354. Esterase_lipase.
    IPR022742. Hydrolase_4.
    [Graphical view]
    PfamiPF12146. Hydrolase_4. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017388. Esterase_lipase. 1 hit.
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q06174-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKIVPPKPFF FEAGERAVLL LHGFTGNSAD VRMLGRFLES KGYTCHAPIY
    60 70 80 90 100
    KGHGVPPEEL VHTGPDDWWQ DVMNGYEFLK NKGYEKIAVA GLSLGGVFSL
    110 120 130 140 150
    KLGYTVPIEG IVTMCAPMYI KSEETMYEGV LEYAREYKKR EGKSEEQIEQ
    160 170 180 190 200
    EMEKFKQTPM KTLKALQELI ADVRDHLDLI YAPTFVVQAR HDEMINPDSA
    210 220 230 240
    NIIYNEIESP VKQIKWYEQS GHVITLDQEK DQLHEDIYAF LESLDW
    Length:246
    Mass (Da):28,256
    Last modified:January 20, 2009 - v2
    Checksum:iAF99719B68A5709A
    GO

    Sequence cautioni

    The sequence AAN81911 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAA02182 differs from that shown. Reason: Erroneous initiation. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D12681 Genomic DNA. Translation: BAA02182.1. Different initiation.
    AY186197 Genomic DNA. Translation: AAN81911.1. Different initiation.
    PIRiJC1374.
    RefSeqiWP_033008930.1. NZ_LQYV01000095.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D12681 Genomic DNA. Translation: BAA02182.1. Different initiation.
    AY186197 Genomic DNA. Translation: AAN81911.1. Different initiation.
    PIRiJC1374.
    RefSeqiWP_033008930.1. NZ_LQYV01000095.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R1DX-ray2.00A/B1-246[»]
    1TQHX-ray1.63A1-246[»]
    ProteinModelPortaliQ06174.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    ESTHERigeost-est30. CarbLipBact_1.
    MEROPSiS09.946.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.1.1.1. 623.
    SABIO-RKQ06174.

    Miscellaneous databases

    EvolutionaryTraceiQ06174.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR012354. Esterase_lipase.
    IPR022742. Hydrolase_4.
    [Graphical view]
    PfamiPF12146. Hydrolase_4. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017388. Esterase_lipase. 1 hit.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiEST_GEOSE
    AccessioniPrimary (citable) accession number: Q06174
    Secondary accession number(s): Q79M83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 20, 2009
    Last modified: July 6, 2016
    This is version 88 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.