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Protein

Endochitinase B1

Gene

chiB1

Organism
Neosartorya fumigata (Aspergillus fumigatus)
Status
Reviewed-Annotation score: -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 endo-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

    Keywordsi

    Molecular functionGlycosidase, Hydrolase
    Biological processCarbohydrate 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

    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

    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
    DrugBankiDB04350 Argadin
    DB03632 Argifin

    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...) asparagineSequence 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
    InterProiView protein in InterPro
    IPR011583 Chitinase_II
    IPR029070 Chitinase_insertion_sf
    IPR001223 Glyco_hydro18_cat
    IPR001579 Glyco_hydro_18_chit_AS
    IPR017853 Glycoside_hydrolase_SF
    PfamiView protein in Pfam
    PF00704 Glyco_hydro_18, 1 hit
    SMARTiView protein in SMART
    SM00636 Glyco_18, 1 hit
    SUPFAMiSSF51445 SSF51445, 2 hits
    SSF54556 SSF54556, 1 hit
    PROSITEiView protein in PROSITE
    PS01095 CHITINASE_18, 1 hit

    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

    Similar proteinsi

    Entry informationi

    Entry nameiCHIB1_ASPFM
    AccessioniPrimary (citable) accession number: Q873X9
    Secondary accession number(s): Q4WB85
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 9, 2014
    Last sequence update: June 1, 2003
    Last modified: February 28, 2018
    This is version 104 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

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