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Protein

Endochitinase A1

Gene

chiA1

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

Functioni

GPI-anchored 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). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation.1 Publication

Catalytic activityi

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.2 Publications

Enzyme regulationi

The cyclic peptide natural product argifin acts as a specific inhibitor.1 Publication

Kineticsi

  1. KM=300 µM for 4-methylumbelliferyl beta-D-N,N'-diacetylchitobiose1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei34 – 341Inhibitor1 Publication
    Binding sitei124 – 1241Inhibitor; via amide nitrogen1 Publication
    Binding sitei125 – 1251Inhibitor1 Publication
    Active sitei174 – 1741Proton donorPROSITE-ProRule annotation
    Binding sitei207 – 2071Inhibitor1 Publication
    Binding sitei312 – 3121Inhibitor1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

    Keywords - Ligandi

    Chitin-binding

    Protein family/group databases

    CAZyiGH18. Glycoside Hydrolase Family 18.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endochitinase A1 (EC:3.2.1.14)
    Alternative name(s):
    Chitinase A1
    Gene namesi
    Name:chiA1
    Synonyms:chi1
    OrganismiNeosartorya fumigata (Aspergillus fumigatus)
    Taxonomic identifieri746128 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cell wall, Membrane, Secreted

    Pathology & Biotechi

    Chemistry

    ChEMBLiCHEMBL1293196.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence analysisAdd
    BLAST
    Chaini23 – 800778Endochitinase A1PRO_0000429814Add
    BLAST
    Propeptidei801 – 82525Removed in mature formSequence analysisPRO_0000429815Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi559 – 5591N-linked (GlcNAc...)Sequence analysis
    Glycosylationi717 – 7171N-linked (GlcNAc...)Sequence analysis
    Lipidationi800 – 8001GPI-anchor amidated glycineSequence analysis

    Post-translational modificationi

    O-mannosylated by pmt4.

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Expressioni

    Inductioni

    Shows high levels of constitutive expression and repressed by caspofungin.2 Publications

    Interactioni

    Chemistry

    BindingDBiQ873Y0.

    Structurei

    Secondary structure

    1
    825
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 367Combined sources
    Helixi44 – 485Combined sources
    Beta strandi55 – 617Combined sources
    Helixi65 – 673Combined sources
    Helixi69 – 713Combined sources
    Helixi78 – 803Combined sources
    Beta strandi85 – 873Combined sources
    Beta strandi93 – 975Combined sources
    Helixi101 – 11212Combined sources
    Beta strandi116 – 12712Combined sources
    Helixi134 – 14815Combined sources
    Turni160 – 1634Combined sources
    Beta strandi167 – 1737Combined sources
    Helixi181 – 19313Combined sources
    Beta strandi201 – 2044Combined sources
    Beta strandi207 – 2115Combined sources
    Turni213 – 2153Combined sources
    Helixi216 – 2216Combined sources
    Beta strandi225 – 2306Combined sources
    Helixi235 – 2373Combined sources
    Helixi240 – 2423Combined sources
    Helixi252 – 2609Combined sources
    Turni263 – 2664Combined sources
    Beta strandi268 – 2769Combined sources
    Helixi277 – 2793Combined sources
    Helixi288 – 30114Combined sources
    Turni303 – 3053Combined sources
    Beta strandi306 – 3127Combined sources
    Helixi314 – 3196Combined sources
    Helixi327 – 33610Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XUCX-ray2.30A/B/C29-337[»]
    2XVNX-ray2.35A/B/C29-337[»]
    ProteinModelPortaliQ873Y0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ873Y0.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni170 – 1745Inhibitor binding
    Regioni230 – 2323Inhibitor binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi346 – 689344Ser/Thr-richAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001223. 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]
    SUPFAMiSSF51445. SSF51445. 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.

    Q873Y0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVSSKLSFVA TAVAALAPLA SAFDASSRSN LAIYWGQGPN QLRLSHFCQE
    60 70 80 90 100
    TSLDIINIGF INYFPDMSPG HWPGSNFGNQ CDGSVYVTND GVVTKLLSGC
    110 120 130 140 150
    HQIMEDIPIC QAAGKKVLLS IGGAYPPDQS ILSEDSAVAF ATFLWGAFGP
    160 170 180 190 200
    VAEGWEGPRP FGDVVVDGFD FDIEHNGGFG YATMVNTFRQ YFNQVPERKF
    210 220 230 240 250
    YLSAAPQCII PDAQLSDAIF NAAFDFIWIQ YYNTAACSAK SFIDTSLGTF
    260 270 280 290 300
    NFDAWVTVLK ASASKDAKLY VGLPASETAA NQGYYLTPDE VESLVSTYMD
    310 320 330 340 350
    RYPDTFGGIM LWEATASENN QIDGAPYADH MKDILLHCDP SPPVTSSSAV
    360 370 380 390 400
    PSSTPVTTPS PSSSAVPSST PAVSETPSPS SSAVPSSTPV ASSTPVVPGT
    410 420 430 440 450
    SASSSPVSSS SAIAPSTPVV PGTSTPSSTP VASSTPVVPG TSASSSPVSS
    460 470 480 490 500
    SSAVASSTPV VPGTSVPSST PAIPGGSSSS SEAVASSTPL VTLTLTVSPT
    510 520 530 540 550
    PAPSSSESSS TDLSSSTQTD VGTAPSQPAG PSTTATATTS SSSSSTDESS
    560 570 580 590 600
    TTVGSGNGNG SGSTTTTAAT DSITAAPTAT SSATATGATS EPVTITTIIV
    610 620 630 640 650
    TSYIDICPTG FTTVTTTYTT TYCPGTNTAT ATATVTNPPS GPGGAGSQTT
    660 670 680 690 700
    APTVPEGWTT TVTVCTQCAA KPTTVTLTLP VTETGSTSTD AVPAPPAATG
    710 720 730 740 750
    EGSNPTQPSG ASPTGGNGSF SEEPVPPPAV TQVSTSTEIV TLVRPTSSRP
    760 770 780 790 800
    LILGTGTVHP SSTLAVKPSA KPSGQNSGSS SHVPIPPSYT QEAVSPLSTG
    810 820
    AASRVTGLGH GLVLTVLTLS AFFVL
    Length:825
    Mass (Da):83,088
    Last modified:June 1, 2003 - v1
    Checksum:i8C2017A8FD1A208C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY217659 Genomic DNA. Translation: AAO61685.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY217659 Genomic DNA. Translation: AAO61685.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XUCX-ray2.30A/B/C29-337[»]
    2XVNX-ray2.35A/B/C29-337[»]
    ProteinModelPortaliQ873Y0.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry

    BindingDBiQ873Y0.
    ChEMBLiCHEMBL1293196.

    Protein family/group databases

    CAZyiGH18. Glycoside Hydrolase Family 18.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ873Y0.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001223. 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]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS01095. CHITINASE_18. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Disruption of the gene encoding the ChiB1 chitinase of Aspergillus fumigatus and characterization of a recombinant gene product."
      Jaques A.K., Fukamizo T., Hall D., Barton R.C., Escott G.M., Parkinson T., Hitchcock C.A., Adams D.J.
      Microbiology 149:2931-2939(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NIH 5233 / ATCC 13073.
    2. "Differential expression and extent of fungal/plant and fungal/bacterial chitinases of Aspergillus fumigatus."
      Taib M., Pinney J.W., Westhead D.R., McDowall K.J., Adams D.J.
      Arch. Microbiol. 184:78-81(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
    3. "Members of protein O-mannosyltransferase family in Aspergillus fumigatus differentially affect growth, morphogenesis and viability."
      Mouyna I., Kniemeyer O., Jank T., Loussert C., Mellado E., Aimanianda V., Beauvais A., Wartenberg D., Sarfati J., Bayry J., Prevost M.C., Brakhage A.A., Strahl S., Huerre M., Latge J.P.
      Mol. Microbiol. 76:1205-1221(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    4. "Profiling the Aspergillus fumigatus proteome in response to caspofungin."
      Cagas S.E., Jain M.R., Li H., Perlin D.S.
      Antimicrob. Agents Chemother. 55:146-154(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INDUCTION.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 29-337 IN COMPLEX WITH INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

    Entry informationi

    Entry nameiCHIA1_ASPFM
    AccessioniPrimary (citable) accession number: Q873Y0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 9, 2014
    Last sequence update: June 1, 2003
    Last modified: September 16, 2015
    This is version 68 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.