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Protein

Acetylxylan esterase / glucomannan deacetylase

Gene

axe2C

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 equal efficiency, and of the synthetic substrate 4-nitrophenyl acetate (4-NPAc). Does not bind cellulose, cellohexaose and beta-glucan.1 Publication

Catalytic activityi

Deacetylation of xylans and xylo-oligosaccharides.1 Publication

Kineticsi

kcat is 7717 min(-1) for the deacetylation of 4-nitrophenyl acetate. kcat is 69 min(-1) for the deacetylation of birchwood xylan. kcat is 163 min(-1) for the deacetylation of glucomannan.1 Publication

  1. KM=339 µM for 4-nitrophenyl acetate1 Publication
  2. KM=1.5 mM for acetylated birchwood xylan1 Publication
  3. KM=4.2 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 sitei160 – 1601Nucleophile1 Publication
    Sitei205 – 2051Transition state stabilizer1 Publication
    Sitei255 – 2551Transition state stabilizer1 Publication
    Active sitei333 – 3331Charge relay system1 Publication
    Active sitei335 – 3351Charge relay system1 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-450-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):
    CjCE2A1 Publication
    Gene namesi
    Name:axe2CImported
    Ordered Locus Names:CJA_0450Imported
    OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
    Taxonomic identifieri498211 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
    Proteomesi
    • UP000001036 Componenti: Chromosome

    Subcellular locationi

    • Cell membrane PROSITE-ProRule annotation; Lipid-anchor PROSITE-ProRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818PROSITE-ProRule annotationAdd
    BLAST
    Chaini19 – 358340Acetylxylan esterase / glucomannan deacetylasePRO_0000434123Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi19 – 191N-palmitoyl cysteinePROSITE-ProRule annotation
    Lipidationi19 – 191S-diacylglycerol cysteinePROSITE-ProRule annotation

    Keywords - PTMi

    Lipoprotein, Palmitate

    Interactioni

    Protein-protein interaction databases

    STRINGi498211.CJA_0450.

    Structurei

    Secondary structure

    1
    358
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 368Combined sources
    Beta strandi39 – 435Combined sources
    Beta strandi53 – 553Combined sources
    Beta strandi61 – 8020Combined sources
    Beta strandi82 – 887Combined sources
    Beta strandi94 – 985Combined sources
    Beta strandi103 – 12220Combined sources
    Helixi126 – 1283Combined sources
    Beta strandi131 – 14313Combined sources
    Beta strandi151 – 1599Combined sources
    Turni160 – 1689Combined sources
    Helixi177 – 1793Combined sources
    Helixi186 – 1938Combined sources
    Beta strandi196 – 2027Combined sources
    Beta strandi216 – 2183Combined sources
    Helixi221 – 2244Combined sources
    Beta strandi227 – 2293Combined sources
    Helixi240 – 2423Combined sources
    Beta strandi246 – 2505Combined sources
    Helixi254 – 2574Combined sources
    Beta strandi258 – 2603Combined sources
    Helixi264 – 28118Combined sources
    Beta strandi286 – 2894Combined sources
    Helixi297 – 31418Combined sources
    Beta strandi319 – 3213Combined sources
    Beta strandi333 – 3353Combined sources
    Helixi338 – 35619Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WAAX-ray1.80A21-358[»]
    ProteinModelPortaliB3PIB0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiB3PIB0.

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4108PC0. Bacteria.
    ENOG4111J8W. LUCA.
    HOGENOMiHOG000066292.
    OMAiRIANTFD.
    OrthoDBiEOG6GTZK9.

    Family and domain databases

    Gene3Di3.40.50.1110. 1 hit.
    InterProiIPR013830. SGNH_hydro.
    [Graphical view]
    PfamiPF13472. Lipase_GDSL_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52266. SSF52266. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    B3PIB0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLLFPILLL TGSYFLSACN NTQSLMSSTH TIAASDPHIQ VMGRTHINDD
    60 70 80 90 100
    ASLTFGYPGV SLSTIVAGSR LTAEMQSSNG NSWIDVIIDN HPPTSIKLDA
    110 120 130 140 150
    QQQTVELFHF PNSGEHRVEI IHRSENWHGQ VTLKQLTLTG TQFLPAPVLP
    160 170 180 190 200
    QRKILVLGDS VTCGEAIDRV AGEDKNTRWW NARESYGMLT AKALDAQVQL
    210 220 230 240 250
    VCWGGRGLIR SWNGKTDDAN LPDFYQFTLG DTGQAPQWDH HRYQPDLIIS
    260 270 280 290 300
    AIGTNDFSPG IPDRATYINT YTRFVRTLLD NHPQATIVLT EGAILNGDKK
    310 320 330 340 350
    AALVSYIGET RQQLHSNRVF YASSSHHPGD NSDAHPTKDQ HAAMARELTP

    QLRQIMDW
    Length:358
    Mass (Da):39,779
    Last modified:September 2, 2008 - v1
    Checksum:iC12DB2C29F4B819E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000934 Genomic DNA. Translation: ACE84991.1.
    RefSeqiWP_012486130.1. NC_010995.1.

    Genome annotation databases

    EnsemblBacteriaiACE84991; ACE84991; CJA_0450.
    KEGGicja:CJA_0450.
    PATRICi21324281. VBICelJap122165_0460.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000934 Genomic DNA. Translation: ACE84991.1.
    RefSeqiWP_012486130.1. NC_010995.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WAAX-ray1.80A21-358[»]
    ProteinModelPortaliB3PIB0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi498211.CJA_0450.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiACE84991; ACE84991; CJA_0450.
    KEGGicja:CJA_0450.
    PATRICi21324281. VBICelJap122165_0460.

    Phylogenomic databases

    eggNOGiENOG4108PC0. Bacteria.
    ENOG4111J8W. LUCA.
    HOGENOMiHOG000066292.
    OMAiRIANTFD.
    OrthoDBiEOG6GTZK9.

    Enzyme and pathway databases

    UniPathwayiUPA00114.
    BioCyciCJAP498211:GHIT-450-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiB3PIB0.

    Family and domain databases

    Gene3Di3.40.50.1110. 1 hit.
    InterProiIPR013830. SGNH_hydro.
    [Graphical view]
    PfamiPF13472. Lipase_GDSL_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52266. SSF52266. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
      DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
      J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ueda107.
    2. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 21-358, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE.

    Entry informationi

    Entry nameiCE2A_CELJU
    AccessioniPrimary (citable) accession number: B3PIB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 14, 2015
    Last sequence update: September 2, 2008
    Last modified: December 9, 2015
    This is version 49 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.