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Protein

Acetylxylan esterase / glucomannan deacetylase

Gene

ce2C

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of plant cell wall polysaccharides. Catalyzes the deacetylation of acetylated birchwood xylan and glucomannan, with a large preference for the latter, and of the synthetic substrate 4-nitrophenyl acetate (4-NPAc).1 Publication

Catalytic activityi

Deacetylation of xylans and xylo-oligosaccharides.1 Publication

Kineticsi

kcat is 49820 min(-1) for the deacetylation of 4-nitrophenyl acetate. kcat is 66 min(-1) for the deacetylation of birchwood xylan. kcat is 1348 min(-1) for the deacetylation of glucomannan.1 Publication

  1. KM=262 µM for 4-nitrophenyl acetate1 Publication
  2. KM=4.6 mM for acetylated birchwood xylan1 Publication
  3. KM=0.84 mM for acetylated glucomannan1 Publication

    Pathwayi: xylan degradation

    This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.1 Publication
    View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei151 – 1511Nucleophile1 Publication
    Sitei199 – 1991Transition state stabilizerBy similarity
    Sitei247 – 2471Transition state stabilizerBy similarity
    Sitei336 – 3361Increases nucleophilicity of active site Ser1 Publication

    GO - Molecular functioni

    • acetylxylan esterase activity Source: UniProtKB
    • hydrolase activity, acting on glycosyl bonds Source: UniProtKB-KW

    GO - Biological processi

    • glucomannan catabolic process Source: UniProtKB
    • xylan catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciCJAP498211:GHIT-3093-MONOMER.
    UniPathwayiUPA00114.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylxylan esterase / glucomannan deacetylase1 Publication (EC:3.1.1.-1 Publication, EC:3.1.1.721 Publication)
    Alternative name(s):
    CjCE2B1 Publication
    Gene namesi
    Name:ce2CImported
    Ordered Locus Names:CJA_3103Imported
    OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
    Taxonomic identifieri498211 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
    Proteomesi
    • UP000001036 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence analysisAdd
    BLAST
    Chaini22 – 360339Acetylxylan esterase / glucomannan deacetylasePRO_0000434124Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi498211.CJA_3103.

    Structurei

    Secondary structure

    1
    360
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 344Combined sources
    Beta strandi37 – 393Combined sources
    Beta strandi47 – 504Combined sources
    Beta strandi56 – 594Combined sources
    Beta strandi68 – 747Combined sources
    Beta strandi76 – 805Combined sources
    Beta strandi87 – 904Combined sources
    Beta strandi93 – 975Combined sources
    Beta strandi109 – 1135Combined sources
    Beta strandi122 – 1243Combined sources
    Beta strandi144 – 1507Combined sources
    Helixi151 – 1544Combined sources
    Turni155 – 1595Combined sources
    Helixi167 – 1737Combined sources
    Helixi176 – 1783Combined sources
    Helixi180 – 1878Combined sources
    Beta strandi191 – 1966Combined sources
    Helixi206 – 2083Combined sources
    Helixi215 – 2184Combined sources
    Beta strandi221 – 2255Combined sources
    Beta strandi238 – 2436Combined sources
    Helixi246 – 2494Combined sources
    Helixi262 – 28322Combined sources
    Beta strandi288 – 2958Combined sources
    Helixi297 – 2993Combined sources
    Helixi300 – 31415Combined sources
    Beta strandi320 – 3256Combined sources
    Helixi333 – 3353Combined sources
    Helixi339 – 35416Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W9XX-ray2.00A/B1-360[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiB3PDE5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the carbohydrate esterase 2 (CE2) family.1 Publication

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4108PC0. Bacteria.
    ENOG4111J8W. LUCA.
    HOGENOMiHOG000140382.
    OMAiRTENYAS.
    OrthoDBiPOG091H09LD.

    Family and domain databases

    Gene3Di3.40.50.1110. 1 hit.
    InterProiIPR001087. GDSL.
    IPR013830. SGNH_hydro.
    [Graphical view]
    PfamiPF00657. Lipase_GDSL. 1 hit.
    [Graphical view]
    SUPFAMiSSF52266. SSF52266. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    B3PDE5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKPHALIGLL AGMLLSSSLY AADSTKPLPL HIGGRVLVES PANQPVSYTY
    60 70 80 90 100
    SWPAVYFETA FKGQSLTLKF DDDQNIFRLI VDDKAPVVIN KPGKVDYPVE
    110 120 130 140 150
    SLAPGKHRVR LEKLTETQST SGRFLGFYTD PSAKPLALPK RKRQIEFIGD
    160 170 180 190 200
    SFTVGYGNTS PSRECTDEEL FKTTNSQMAF GPLTAKAFDA DYQINASSGF
    210 220 230 240 250
    GIVRNYNGTS PDKSLLSLYP YTLNNPDQLY HNKHWKPQVI VIGLGTNDFS
    260 270 280 290 300
    TALNDNERWK TREALHADYV ANYVKFVKQL HSNNARAQFI LMNSDQSNGE
    310 320 330 340 350
    IAEQVGKVVA QLKGGGLHQV EQIVFKGLDY SGCHWHPSAN DDQLLANLLI
    360
    THLQQKKGIW
    Length:360
    Mass (Da):40,063
    Last modified:September 2, 2008 - v1
    Checksum:i6F589FE17E026C9F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000934 Genomic DNA. Translation: ACE85322.1.
    RefSeqiWP_012488681.1. NC_010995.1.

    Genome annotation databases

    EnsemblBacteriaiACE85322; ACE85322; CJA_3103.
    KEGGicja:CJA_3103.
    PATRICi21329599. VBICelJap122165_3064.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000934 Genomic DNA. Translation: ACE85322.1.
    RefSeqiWP_012488681.1. NC_010995.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W9XX-ray2.00A/B1-360[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi498211.CJA_3103.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiACE85322; ACE85322; CJA_3103.
    KEGGicja:CJA_3103.
    PATRICi21329599. VBICelJap122165_3064.

    Phylogenomic databases

    eggNOGiENOG4108PC0. Bacteria.
    ENOG4111J8W. LUCA.
    HOGENOMiHOG000140382.
    OMAiRTENYAS.
    OrthoDBiPOG091H09LD.

    Enzyme and pathway databases

    UniPathwayiUPA00114.
    BioCyciCJAP498211:GHIT-3093-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiB3PDE5.

    Family and domain databases

    Gene3Di3.40.50.1110. 1 hit.
    InterProiIPR001087. GDSL.
    IPR013830. SGNH_hydro.
    [Graphical view]
    PfamiPF00657. Lipase_GDSL. 1 hit.
    [Graphical view]
    SUPFAMiSSF52266. SSF52266. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCE2B_CELJU
    AccessioniPrimary (citable) accession number: B3PDE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 14, 2015
    Last sequence update: September 2, 2008
    Last modified: September 7, 2016
    This is version 45 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.