Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
    Binding sitei34Inhibitor1 Publication1
    Binding sitei124Inhibitor; via amide nitrogen1 Publication1
    Binding sitei125Inhibitor1 Publication1
    Active sitei174Proton donorPROSITE-ProRule annotation1
    Binding sitei207Inhibitor1 Publication1
    Binding sitei312Inhibitor1 Publication1

    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 databases

    ChEMBLiCHEMBL1293196.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 22Sequence analysisAdd BLAST22
    ChainiPRO_000042981423 – 800Endochitinase A1Add BLAST778
    PropeptideiPRO_0000429815801 – 825Removed in mature formSequence analysisAdd BLAST25

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi559N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi717N-linked (GlcNAc...)Sequence analysis1
    Lipidationi800GPI-anchor amidated glycineSequence analysis1

    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 databases

    BindingDBiQ873Y0.

    Structurei

    Secondary structure

    1825
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi30 – 36Combined sources7
    Helixi44 – 48Combined sources5
    Beta strandi55 – 61Combined sources7
    Helixi65 – 67Combined sources3
    Helixi69 – 71Combined sources3
    Helixi78 – 80Combined sources3
    Beta strandi85 – 87Combined sources3
    Beta strandi93 – 97Combined sources5
    Helixi101 – 112Combined sources12
    Beta strandi116 – 127Combined sources12
    Helixi134 – 148Combined sources15
    Turni160 – 163Combined sources4
    Beta strandi167 – 173Combined sources7
    Helixi181 – 193Combined sources13
    Beta strandi201 – 204Combined sources4
    Beta strandi207 – 211Combined sources5
    Turni213 – 215Combined sources3
    Helixi216 – 221Combined sources6
    Beta strandi225 – 230Combined sources6
    Helixi235 – 237Combined sources3
    Helixi240 – 242Combined sources3
    Helixi252 – 260Combined sources9
    Turni263 – 266Combined sources4
    Beta strandi268 – 276Combined sources9
    Helixi277 – 279Combined sources3
    Helixi288 – 301Combined sources14
    Turni303 – 305Combined sources3
    Beta strandi306 – 312Combined sources7
    Helixi314 – 319Combined sources6
    Helixi327 – 336Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2XUCX-ray2.30A/B/C29-337[»]
    2XVNX-ray2.35A/B/C29-337[»]
    ProteinModelPortaliQ873Y0.
    SMRiQ873Y0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ873Y0.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni170 – 174Inhibitor binding5
    Regioni230 – 232Inhibitor binding3

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi346 – 689Ser/Thr-richAdd BLAST344

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2XUCX-ray2.30A/B/C29-337[»]
    2XVNX-ray2.35A/B/C29-337[»]
    ProteinModelPortaliQ873Y0.
    SMRiQ873Y0.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    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...

    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: November 2, 2016
    This is version 69 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.