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Protein

Endochitinase B1

Gene

chiB1

Organism
Neosartorya fumigata (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a role in the morphogenesis and autolysis (By similarity).By similarity

Catalytic activityi

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.5 Publications

Enzyme regulationi

Methylxanthine drugs surch as theophylline, caffeine and pentoxifylline, as well as the two cyclic peptide natural products argifin and argadin, act as specific inhibitors.4 Publications

Kineticsi

  1. KM=19.9 µM for 4-methylumbelliferyl beta-D-N,N'-diacetylchitobiose2 Publications
  2. KM=2.94 mg/ml for chitosan2 Publications

    pH dependencei

    Optimum pH is 5.0-7.0.2 Publications

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521Inhibitor5 Publications
    Binding sitei137 – 1371Inhibitor; via amide nitrogen5 Publications
    Active sitei177 – 1771Proton donorPROSITE-ProRule annotation
    Binding sitei245 – 2451Inhibitor5 Publications
    Binding sitei246 – 2461Inhibitor5 Publications
    Binding sitei251 – 2511Inhibitor; via amide nitrogen5 Publications
    Binding sitei301 – 3011Inhibitor5 Publications
    Binding sitei322 – 3221Inhibitor5 Publications
    Binding sitei384 – 3841Inhibitor5 Publications

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH18. Glycoside Hydrolase Family 18.
    mycoCLAPiCHI18A_ASPFU.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endochitinase B1 (EC:3.2.1.14)
    Alternative name(s):
    Chitinase B1
    Gene namesi
    Name:chiB1
    OrganismiNeosartorya fumigata (Aspergillus fumigatus)
    Taxonomic identifieri746128 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Decreases the level of chitinase activity during the autolytic phase of batch cultures.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi137 – 1371W → A: Affects substrate-binding and completely abrogates argifin/argadin-binding. 3 Publications
    Mutagenesisi138 – 1381T → A: Affects binding to argifin and argadin. 2 Publications
    Mutagenesisi175 – 1751D → A: Impairs catalytic activity and decreases argifin/argadin-binding but not substrate-binding. 2 Publications
    Mutagenesisi177 – 1771E → A: Impairs catalytic activity and decreases argifin/argadin-binding but not substrate-binding. 2 Publications
    Mutagenesisi217 – 2171A → G: Affects binding to argifin. 2 Publications
    Mutagenesisi243 – 2431M → A: Affects binding to argadin. 3 Publications
    Mutagenesisi245 – 2451Y → F: Impairs catalytic activity and decreases argifin/argadin-binding but not substrate-binding. 2 Publications
    Mutagenesisi246 – 2461D → A: Impairs catalytic activity and decreases argifin/argadin-binding but not substrate-binding. 3 Publications
    Mutagenesisi251 – 2511F → A: Affects substrate-binding and completely abrogates argifin/argadin-binding. 1 Publication
    Mutagenesisi301 – 3011R → K: Impairs catalytic activity but not substrate-binding. 2 Publications
    Mutagenesisi322 – 3221E → A: Affects binding to argifin and argadin. 2 Publications

    Chemistry

    ChEMBLiCHEMBL4638.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence analysisAdd
    BLAST
    Chaini23 – 433411Endochitinase B1PRO_0000429823Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence analysis

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Inductioni

    Induced during batch culture.1 Publication

    Interactioni

    Chemistry

    BindingDBiQ873X9.

    Structurei

    Secondary structure

    1
    433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 508Combined sources
    Helixi51 – 544Combined sources
    Helixi61 – 633Combined sources
    Helixi66 – 683Combined sources
    Beta strandi70 – 7910Combined sources
    Turni81 – 833Combined sources
    Beta strandi86 – 894Combined sources
    Helixi91 – 955Combined sources
    Helixi113 – 12412Combined sources
    Beta strandi129 – 1357Combined sources
    Turni137 – 1393Combined sources
    Helixi140 – 1423Combined sources
    Helixi143 – 1475Combined sources
    Helixi150 – 16718Combined sources
    Beta strandi170 – 1756Combined sources
    Helixi182 – 20625Combined sources
    Beta strandi207 – 2093Combined sources
    Beta strandi213 – 2186Combined sources
    Helixi222 – 2276Combined sources
    Helixi230 – 2345Combined sources
    Beta strandi238 – 2425Combined sources
    Beta strandi247 – 2493Combined sources
    Beta strandi252 – 2543Combined sources
    Helixi268 – 2703Combined sources
    Helixi275 – 28410Combined sources
    Helixi289 – 2913Combined sources
    Beta strandi292 – 30514Combined sources
    Beta strandi320 – 3223Combined sources
    Beta strandi325 – 3273Combined sources
    Helixi328 – 3303Combined sources
    Beta strandi337 – 3415Combined sources
    Helixi342 – 3443Combined sources
    Beta strandi346 – 3516Combined sources
    Turni352 – 3554Combined sources
    Beta strandi356 – 3594Combined sources
    Helixi363 – 37614Combined sources
    Beta strandi380 – 3845Combined sources
    Helixi386 – 3883Combined sources
    Helixi392 – 3943Combined sources
    Helixi396 – 4038Combined sources
    Helixi407 – 4093Combined sources
    Helixi425 – 4284Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W9PX-ray1.70A/B1-433[»]
    1W9UX-ray1.85A/B1-433[»]
    1W9VX-ray2.00A/B1-433[»]
    1WNOX-ray2.10A/B39-433[»]
    2A3AX-ray2.10A/B1-433[»]
    2A3BX-ray1.90A/B1-433[»]
    2A3CX-ray2.07A/B1-433[»]
    2A3EX-ray1.95A/B1-433[»]
    2IUZX-ray1.95A/B1-433[»]
    3CH9X-ray2.20A/B1-433[»]
    3CHCX-ray1.90A/B1-433[»]
    3CHDX-ray2.00A/B1-433[»]
    3CHEX-ray2.05A/B1-433[»]
    3CHFX-ray1.95A/B1-433[»]
    ProteinModelPortaliQ873X9.
    SMRiQ873X9. Positions 39-433.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ873X9.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni175 – 1773Inhibitor binding

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000169884.

    Family and domain databases

    Gene3Di3.10.50.10. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR011583. Chitinase_II.
    IPR029070. Chitinase_insertion.
    IPR001223. Glyco_hydro18_cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00704. Glyco_hydro_18. 1 hit.
    [Graphical view]
    SMARTiSM00636. Glyco_18. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    SSF54556. SSF54556. 1 hit.
    PROSITEiPS01095. CHITINASE_18. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q873X9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRFATSTIVK VALLLSSLCV DAAVMWNRDT SSTDLEARAS SGYRSVVYFV
    60 70 80 90 100
    NWAIYGRNHN PQDLPVERLT HVLYAFANVR PETGEVYMTD SWADIEKHYP
    110 120 130 140 150
    GDSWSDTGNN VYGCIKQLYL LKKQNRNLKV LLSIGGWTYS PNFAPAASTD
    160 170 180 190 200
    AGRKNFAKTA VKLLQDLGFD GLDIDWEYPE NDQQANDFVL LLKEVRTALD
    210 220 230 240 250
    SYSAANAGGQ HFLLTVASPA GPDKIKVLHL KDMDQQLDFW NLMAYDYAGS
    260 270 280 290 300
    FSSLSGHQAN VYNDTSNPLS TPFNTQTALD LYRAGGVPAN KIVLGMPLYG
    310 320 330 340 350
    RSFANTDGPG KPYNGVGQGS WENGVWDYKA LPQAGATEHV LPDIMASYSY
    360 370 380 390 400
    DATNKFLISY DNPQVANLKS GYIKSLGLGG AMWWDSSSDK TGSDSLITTV
    410 420 430
    VNALGGTGVF EQSQNELDYP VSQYDNLRNG MQT
    Length:433
    Mass (Da):47,622
    Last modified:June 1, 2003 - v1
    Checksum:i95AECA3DCE917D30
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY217660 Genomic DNA. Translation: AAO61686.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY217660 Genomic DNA. Translation: AAO61686.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W9PX-ray1.70A/B1-433[»]
    1W9UX-ray1.85A/B1-433[»]
    1W9VX-ray2.00A/B1-433[»]
    1WNOX-ray2.10A/B39-433[»]
    2A3AX-ray2.10A/B1-433[»]
    2A3BX-ray1.90A/B1-433[»]
    2A3CX-ray2.07A/B1-433[»]
    2A3EX-ray1.95A/B1-433[»]
    2IUZX-ray1.95A/B1-433[»]
    3CH9X-ray2.20A/B1-433[»]
    3CHCX-ray1.90A/B1-433[»]
    3CHDX-ray2.00A/B1-433[»]
    3CHEX-ray2.05A/B1-433[»]
    3CHFX-ray1.95A/B1-433[»]
    ProteinModelPortaliQ873X9.
    SMRiQ873X9. Positions 39-433.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry

    BindingDBiQ873X9.
    ChEMBLiCHEMBL4638.

    Protein family/group databases

    CAZyiGH18. Glycoside Hydrolase Family 18.
    mycoCLAPiCHI18A_ASPFU.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    HOGENOMiHOG000169884.

    Miscellaneous databases

    EvolutionaryTraceiQ873X9.

    Family and domain databases

    Gene3Di3.10.50.10. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR011583. Chitinase_II.
    IPR029070. Chitinase_insertion.
    IPR001223. Glyco_hydro18_cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00704. Glyco_hydro_18. 1 hit.
    [Graphical view]
    SMARTiSM00636. Glyco_18. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    SSF54556. SSF54556. 1 hit.
    PROSITEiPS01095. CHITINASE_18. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCHIB1_ASPFM
    AccessioniPrimary (citable) accession number: Q873X9
    Secondary accession number(s): Q4WB85
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 9, 2014
    Last sequence update: June 1, 2003
    Last modified: October 14, 2015
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    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.