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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Active sitei151Nucleophile1 Publication1
    Sitei199Transition state stabilizerBy similarity1
    Sitei247Transition state stabilizerBy similarity1
    Sitei336Increases nucleophilicity of active site Ser1 Publication1

    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

    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)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 21Sequence analysisAdd BLAST21
    ChainiPRO_000043412422 – 360Acetylxylan esterase / glucomannan deacetylaseAdd BLAST339

    Interactioni

    Protein-protein interaction databases

    STRINGi498211.CJA_3103.

    Structurei

    Secondary structure

    1360
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi31 – 34Combined sources4
    Beta strandi37 – 39Combined sources3
    Beta strandi47 – 50Combined sources4
    Beta strandi56 – 59Combined sources4
    Beta strandi68 – 74Combined sources7
    Beta strandi76 – 80Combined sources5
    Beta strandi87 – 90Combined sources4
    Beta strandi93 – 97Combined sources5
    Beta strandi109 – 113Combined sources5
    Beta strandi122 – 124Combined sources3
    Beta strandi144 – 150Combined sources7
    Helixi151 – 154Combined sources4
    Turni155 – 159Combined sources5
    Helixi167 – 173Combined sources7
    Helixi176 – 178Combined sources3
    Helixi180 – 187Combined sources8
    Beta strandi191 – 196Combined sources6
    Helixi206 – 208Combined sources3
    Helixi215 – 218Combined sources4
    Beta strandi221 – 225Combined sources5
    Beta strandi238 – 243Combined sources6
    Helixi246 – 249Combined sources4
    Helixi262 – 283Combined sources22
    Beta strandi288 – 295Combined sources8
    Helixi297 – 299Combined sources3
    Helixi300 – 314Combined sources15
    Beta strandi320 – 325Combined sources6
    Helixi333 – 335Combined sources3
    Helixi339 – 354Combined sources16

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2W9XX-ray2.00A/B1-360[»]
    SMRiB3PDE5.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2W9XX-ray2.00A/B1-360[»]
    SMRiB3PDE5.
    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.

    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: November 2, 2016
    This is version 46 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.