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Protein

1,4-beta-D-glucan cellobiohydrolase xynA

Gene

xynA

Organism
Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.1 Publication

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.1 Publication

Enzyme regulationi

Cellobiose inhibits xynA at high concentrations.1 Publication

Kineticsi

  1. KM=0.238 mM for 4-nitrophenyl-beta-D-cellobioside1 Publication
  2. KM=0.57 mM for 4-nitrophenyl-beta-D-lactopyranoside1 Publication

    pH dependencei

    Optimum pH is 3.0-4.5.1 Publication

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei234NucleophileBy similarity1
    Active sitei239Proton donorBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionGlycosidase, Hydrolase
    Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiCBM1. Carbohydrate-Binding Module Family 1.
    GH7. Glycoside Hydrolase Family 7.
    mycoCLAPiCBH7A_PENFN.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1,4-beta-D-glucan cellobiohydrolase xynA (EC:3.2.1.91)
    Alternative name(s):
    Beta-glucancellobiohydrolase xynA
    Exocellobiohydrolase xynA
    Exoglucanase xynA
    Gene namesi
    Name:xynA
    OrganismiTalaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum)
    Taxonomic identifieri28572 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 25Sequence analysisAdd BLAST25
    ChainiPRO_500006749926 – 5291,4-beta-D-glucan cellobiohydrolase xynAAdd BLAST504

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi70N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi219N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi413N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi455N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi501 ↔ 518By similarity
    Disulfide bondi512 ↔ 528By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ8WZJ4.
    SMRiQ8WZJ4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini493 – 529CBM1PROSITE-ProRule annotationAdd BLAST37

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni26 – 456CatalyticBy similarityAdd BLAST431
    Regioni457 – 493Thr-rich linkerBy similarityAdd BLAST37

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi457 – 519Thr-richAdd BLAST63

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    CDDicd07999. GH7_CBH_EG. 1 hit.
    Gene3Di2.70.100.10. 1 hit.
    InterProiView protein in InterPro
    IPR035971. CBD_sf.
    IPR000254. Cellulose-bd_dom_fun.
    IPR013320. ConA-like_dom_sf.
    IPR001722. Glyco_hydro_7.
    IPR037019. Glyco_hydro_7_sf.
    PANTHERiPTHR33753. PTHR33753. 1 hit.
    PfamiView protein in Pfam
    PF00734. CBM_1. 1 hit.
    PF00840. Glyco_hydro_7. 1 hit.
    PRINTSiPR00734. GLHYDRLASE7.
    ProDomiView protein in ProDom or Entries sharing at least one domain
    PD001821. CBD_fun. 1 hit.
    SMARTiView protein in SMART
    SM00236. fCBD. 1 hit.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEiView protein in PROSITE
    PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q8WZJ4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSALNSFNMY KSALILGSLL ATAGAQQIGT YTAETHPSLS WSTCKSGGSC
    60 70 80 90 100
    TTNSGAITLD ANWRWVHGVN TSTNCYTGNT WNTAICDTDA SCAQDCALDG
    110 120 130 140 150
    ADYSGTYGIT TSGNSLRLNF VTGSNVGSRT YLMADNTHYQ IFDLLNQEFT
    160 170 180 190 200
    FTVDVSNLPC GLNGALYFVT MDADGGVSKY PNNKAGAQYG VGYCDSQCPR
    210 220 230 240 250
    DLKFIAGQAN VEGWTPSTNN SNTGIGNHGS CCAELDIWEA NSISEALTPH
    260 270 280 290 300
    PCDTPGLTVC TADDCGGTYS SNRYAGTCDP DGCDFNPYRL GVTDFYGSGK
    310 320 330 340 350
    TVDTTKPFTV VTQFVTDDGT SSGSLSEIRR YYVQNGVVIP QPSSKISGIS
    360 370 380 390 400
    GNVINSDFCA AELSAFGETA SFTNHGGLKN MGSALEAGMV LVMSLWDDYS
    410 420 430 440 450
    VNMLWLDSTY PANETGTPGA ARGSCPTTSG NPKTVESQSG SSYVVFSDIK
    460 470 480 490 500
    VGPFNSTFSG GTSTGGSTTT TASGTTSTKA STTSTSSTST GTGVAAHWGQ
    510 520
    CGGQGWTGPT TCASGTTCTV VNPYYSQCL
    Length:529
    Mass (Da):55,048
    Last modified:March 1, 2002 - v1
    Checksum:i95232F53577B6416
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ312295 Genomic DNA. Translation: CAC85737.1.

    Similar proteinsi

    Entry informationi

    Entry nameiXYNA_TALFU
    AccessioniPrimary (citable) accession number: Q8WZJ4
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 9, 2014
    Last sequence update: March 1, 2002
    Last modified: December 20, 2017
    This is version 65 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally identified as a 1,4-beta-D-xylan xylanohydrolase (PubMed:12664153). However, further sequence comparisons and enzymatic studies showed that xynA was principally an 1,4-beta-D-glucan cellobiohydrolase (PubMed:22776993).2 Publications

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families