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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)DescriptionActionsGraphical viewLength
    Binding sitei52Inhibitor5 Publications1
    Binding sitei137Inhibitor; via amide nitrogen5 Publications1
    Active sitei177Proton donorPROSITE-ProRule annotation1
    Binding sitei245Inhibitor5 Publications1
    Binding sitei246Inhibitor5 Publications1
    Binding sitei251Inhibitor; via amide nitrogen5 Publications1
    Binding sitei301Inhibitor5 Publications1
    Binding sitei322Inhibitor5 Publications1
    Binding sitei384Inhibitor5 Publications1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi137W → A: Affects substrate-binding and completely abrogates argifin/argadin-binding. 3 Publications1
    Mutagenesisi138T → A: Affects binding to argifin and argadin. 2 Publications1
    Mutagenesisi175D → A: Impairs catalytic activity and decreases argifin/argadin-binding but not substrate-binding. 2 Publications1
    Mutagenesisi177E → A: Impairs catalytic activity and decreases argifin/argadin-binding but not substrate-binding. 2 Publications1
    Mutagenesisi217A → G: Affects binding to argifin. 2 Publications1
    Mutagenesisi243M → A: Affects binding to argadin. 3 Publications1
    Mutagenesisi245Y → F: Impairs catalytic activity and decreases argifin/argadin-binding but not substrate-binding. 2 Publications1
    Mutagenesisi246D → A: Impairs catalytic activity and decreases argifin/argadin-binding but not substrate-binding. 3 Publications1
    Mutagenesisi251F → A: Affects substrate-binding and completely abrogates argifin/argadin-binding. 1 Publication1
    Mutagenesisi301R → K: Impairs catalytic activity but not substrate-binding. 2 Publications1
    Mutagenesisi322E → A: Affects binding to argifin and argadin. 2 Publications1

    Chemistry databases

    ChEMBLiCHEMBL4638.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 22Sequence analysisAdd BLAST22
    ChainiPRO_000042982323 – 433Endochitinase B1Add BLAST411

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi263N-linked (GlcNAc...)Sequence analysis1

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Inductioni

    Induced during batch culture.1 Publication

    Interactioni

    Chemistry databases

    BindingDBiQ873X9.

    Structurei

    Secondary structure

    1433
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi43 – 50Combined sources8
    Helixi51 – 54Combined sources4
    Helixi61 – 63Combined sources3
    Helixi66 – 68Combined sources3
    Beta strandi70 – 79Combined sources10
    Turni81 – 83Combined sources3
    Beta strandi86 – 89Combined sources4
    Helixi91 – 95Combined sources5
    Helixi113 – 124Combined sources12
    Beta strandi129 – 135Combined sources7
    Turni137 – 139Combined sources3
    Helixi140 – 142Combined sources3
    Helixi143 – 147Combined sources5
    Helixi150 – 167Combined sources18
    Beta strandi170 – 175Combined sources6
    Helixi182 – 206Combined sources25
    Beta strandi207 – 209Combined sources3
    Beta strandi213 – 218Combined sources6
    Helixi222 – 227Combined sources6
    Helixi230 – 234Combined sources5
    Beta strandi238 – 242Combined sources5
    Beta strandi247 – 249Combined sources3
    Beta strandi252 – 254Combined sources3
    Helixi268 – 270Combined sources3
    Helixi275 – 284Combined sources10
    Helixi289 – 291Combined sources3
    Beta strandi292 – 305Combined sources14
    Beta strandi320 – 322Combined sources3
    Beta strandi325 – 327Combined sources3
    Helixi328 – 330Combined sources3
    Beta strandi337 – 341Combined sources5
    Helixi342 – 344Combined sources3
    Beta strandi346 – 351Combined sources6
    Turni352 – 355Combined sources4
    Beta strandi356 – 359Combined sources4
    Helixi363 – 376Combined sources14
    Beta strandi380 – 384Combined sources5
    Helixi386 – 388Combined sources3
    Helixi392 – 394Combined sources3
    Helixi396 – 403Combined sources8
    Helixi407 – 409Combined sources3
    Helixi425 – 428Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ873X9.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni175 – 177Inhibitor binding3

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    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: November 2, 2016
    This is version 99 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.