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P20533

- CHIA1_BACCI

UniProt

P20533 - CHIA1_BACCI

Protein

Chitinase A1

Gene

chiA1

Organism
Bacillus circulans
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei204 – 2041Proton donorCurated

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. chitinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. chitin catabolic process Source: UniProtKB-KW
    2. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiCBM12. Carbohydrate-Binding Module Family 12.
    GH18. Glycoside Hydrolase Family 18.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chitinase A1 (EC:3.2.1.14)
    Gene namesi
    Name:chiA1
    OrganismiBacillus circulans
    Taxonomic identifieri1397 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi200 – 2001D → E: No change in activity. 1 Publication
    Mutagenesisi200 – 2001D → N: Decrease in activity. 1 Publication
    Mutagenesisi204 – 2041E → D or Q: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Add
    BLAST
    Chaini42 – 699658Chitinase A1PRO_0000011905Add
    BLAST

    Structurei

    Secondary structure

    1
    699
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 434
    Beta strandi45 – 517
    Helixi52 – 554
    Turni56 – 583
    Helixi62 – 643
    Helixi67 – 693
    Beta strandi71 – 8010
    Beta strandi85 – 884
    Beta strandi97 – 1004
    Beta strandi116 – 1205
    Helixi121 – 1255
    Beta strandi134 – 1374
    Helixi140 – 15112
    Beta strandi156 – 1627
    Beta strandi164 – 1663
    Helixi170 – 1745
    Helixi177 – 19418
    Beta strandi197 – 2026
    Beta strandi206 – 2083
    Helixi220 – 24223
    Beta strandi247 – 2526
    Helixi256 – 2605
    Helixi264 – 2707
    Beta strandi271 – 2766
    Beta strandi286 – 2883
    Helixi299 – 3035
    Turni307 – 3115
    Helixi314 – 32411
    Helixi328 – 3303
    Beta strandi331 – 34414
    Helixi348 – 3514
    Beta strandi357 – 3593
    Beta strandi364 – 3663
    Beta strandi369 – 3713
    Helixi372 – 3787
    Turni379 – 3813
    Beta strandi385 – 3906
    Turni391 – 3944
    Beta strandi395 – 4006
    Turni401 – 4033
    Beta strandi406 – 4083
    Helixi412 – 42514
    Beta strandi429 – 4335
    Helixi435 – 4373
    Helixi442 – 4509
    Beta strandi564 – 5718
    Beta strandi576 – 5816
    Beta strandi587 – 61125
    Beta strandi619 – 62810
    Beta strandi640 – 6434
    Beta strandi658 – 6625
    Beta strandi668 – 6703
    Beta strandi673 – 6753
    Beta strandi681 – 6833
    Turni693 – 6953

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ED7NMR-A655-699[»]
    1ITXX-ray1.10A33-451[»]
    1K85NMR-A559-644[»]
    ProteinModelPortaliP20533.
    SMRiP20533. Positions 33-451, 464-549, 559-644, 655-698.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20533.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini467 – 55387Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini562 – 64786Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni42 – 460419CatalyticAdd
    BLAST

    Sequence similaritiesi

    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.10.10.20. 1 hit.
    2.60.40.10. 2 hits.
    3.10.50.10. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR003610. CBM_fam5/12.
    IPR011583. Chitinase_II.
    IPR029070. Chitinase_insertion.
    IPR003961. Fibronectin_type3.
    IPR001223. Glyco_hydro18cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF02839. CBM_5_12. 1 hit.
    PF00041. fn3. 2 hits.
    PF00704. Glyco_hydro_18. 1 hit.
    [Graphical view]
    SMARTiSM00495. ChtBD3. 1 hit.
    SM00060. FN3. 2 hits.
    SM00636. Glyco_18. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF51055. SSF51055. 1 hit.
    SSF51445. SSF51445. 2 hits.
    SSF54556. SSF54556. 1 hit.
    PROSITEiPS01095. CHITINASE_18. 1 hit.
    PS50853. FN3. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P20533-1 [UniParc]FASTAAdd to Basket

    « Hide

    MINLNKHTAF KKTAKFFLGL SLLLSVIVPS FALQPATAEA ADSYKIVGYY    50
    PSWAAYGRNY NVADIDPTKV THINYAFADI CWNGIHGNPD PSGPNPVTWT 100
    CQNEKSQTIN VPNGTIVLGD PWIDTGKTFA GDTWDQPIAG NINQLNKLKQ 150
    TNPNLKTIIS VGGWTWSNRF SDVAATAATR EVFANSAVDF LRKYNFDGVD 200
    LDWEYPVSGG LDGNSKRPED KQNYTLLLSK IREKLDAAGA VDGKKYLLTI 250
    ASGASATYAA NTELAKIAAI VDWINIMTYD FNGAWQKISA HNAPLNYDPA 300
    ASAAGVPDAN TFNVAAGAQG HLDAGVPAAK LVLGVPFYGR GWDGCAQAGN 350
    GQYQTCTGGS SVGTWEAGSF DFYDLEANYI NKNGYTRYWN DTAKVPYLYN 400
    ASNKRFISYD DAESVGYKTA YIKSKGLGGA MFWELSGDRN KTLQNKLKAD 450
    LPTGGTVPPV DTTAPSVPGN ARSTGVTANS VTLAWNASTD NVGVTGYNVY 500
    NGANLATSVT GTTATISGLT AGTSYTFTIK AKDAAGNLSA ASNAVTVSTT 550
    AQPGGDTQAP TAPTNLASTA QTTSSITLSW TASTDNVGVT GYDVYNGTAL 600
    ATTVTGTTAT ISGLAADTSY TFTVKAKDAA GNVSAASNAV SVKTAAETTN 650
    PGVSAWQVNT AYTAGQLVTY NGKTYKCLQP HTSLAGWEPS NVPALWQLQ 699
    Length:699
    Mass (Da):73,678
    Last modified:February 1, 1991 - v1
    Checksum:iAC7C9B22E2987643
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57601 Genomic DNA. Translation: AAA81528.1.
    PIRiA38368.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57601 Genomic DNA. Translation: AAA81528.1 .
    PIRi A38368.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ED7 NMR - A 655-699 [» ]
    1ITX X-ray 1.10 A 33-451 [» ]
    1K85 NMR - A 559-644 [» ]
    ProteinModelPortali P20533.
    SMRi P20533. Positions 33-451, 464-549, 559-644, 655-698.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM12. Carbohydrate-Binding Module Family 12.
    GH18. Glycoside Hydrolase Family 18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P20533.

    Family and domain databases

    Gene3Di 2.10.10.20. 1 hit.
    2.60.40.10. 2 hits.
    3.10.50.10. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR003610. CBM_fam5/12.
    IPR011583. Chitinase_II.
    IPR029070. Chitinase_insertion.
    IPR003961. Fibronectin_type3.
    IPR001223. Glyco_hydro18cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    Pfami PF02839. CBM_5_12. 1 hit.
    PF00041. fn3. 2 hits.
    PF00704. Glyco_hydro_18. 1 hit.
    [Graphical view ]
    SMARTi SM00495. ChtBD3. 1 hit.
    SM00060. FN3. 2 hits.
    SM00636. Glyco_18. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF51055. SSF51055. 1 hit.
    SSF51445. SSF51445. 2 hits.
    SSF54556. SSF54556. 1 hit.
    PROSITEi PS01095. CHITINASE_18. 1 hit.
    PS50853. FN3. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin."
      Watanabe T., Suzuki K., Oyanagi W., Ohnishi K., Tanaka H.
      J. Biol. Chem. 265:15659-15665(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: WL-12.
    2. "Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity."
      Watanabe T., Kohori K., Miyashita K., Fujii T., Sakai H., Uchida M., Tanaka H.
      J. Biol. Chem. 268:18567-18572(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
      Strain: WL-12.

    Entry informationi

    Entry nameiCHIA1_BACCI
    AccessioniPrimary (citable) accession number: P20533
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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

    External Data

    Dasty 3