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P20533

- CHIA1_BACCI

UniProt

P20533 - CHIA1_BACCI

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Protein

Chitinase A1

Gene

chiA1

Organism
Bacillus circulans
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MINLNKHTAF KKTAKFFLGL SLLLSVIVPS FALQPATAEA ADSYKIVGYY
60 70 80 90 100
PSWAAYGRNY NVADIDPTKV THINYAFADI CWNGIHGNPD PSGPNPVTWT
110 120 130 140 150
CQNEKSQTIN VPNGTIVLGD PWIDTGKTFA GDTWDQPIAG NINQLNKLKQ
160 170 180 190 200
TNPNLKTIIS VGGWTWSNRF SDVAATAATR EVFANSAVDF LRKYNFDGVD
210 220 230 240 250
LDWEYPVSGG LDGNSKRPED KQNYTLLLSK IREKLDAAGA VDGKKYLLTI
260 270 280 290 300
ASGASATYAA NTELAKIAAI VDWINIMTYD FNGAWQKISA HNAPLNYDPA
310 320 330 340 350
ASAAGVPDAN TFNVAAGAQG HLDAGVPAAK LVLGVPFYGR GWDGCAQAGN
360 370 380 390 400
GQYQTCTGGS SVGTWEAGSF DFYDLEANYI NKNGYTRYWN DTAKVPYLYN
410 420 430 440 450
ASNKRFISYD DAESVGYKTA YIKSKGLGGA MFWELSGDRN KTLQNKLKAD
460 470 480 490 500
LPTGGTVPPV DTTAPSVPGN ARSTGVTANS VTLAWNASTD NVGVTGYNVY
510 520 530 540 550
NGANLATSVT GTTATISGLT AGTSYTFTIK AKDAAGNLSA ASNAVTVSTT
560 570 580 590 600
AQPGGDTQAP TAPTNLASTA QTTSSITLSW TASTDNVGVT GYDVYNGTAL
610 620 630 640 650
ATTVTGTTAT ISGLAADTSY TFTVKAKDAA GNVSAASNAV SVKTAAETTN
660 670 680 690
PGVSAWQVNT AYTAGQLVTY NGKTYKCLQP HTSLAGWEPS NVPALWQLQ
Length:699
Mass (Da):73,678
Last modified:February 1, 1991 - v1
Checksum:iAC7C9B22E2987643
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57601 Genomic DNA. Translation: AAA81528.1.
PIRiA38368.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57601 Genomic DNA. Translation: AAA81528.1 .
PIRi A38368.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 108 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