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Protein

Endochitinase B

Gene

chiB

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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. Has also significant antifungal activity against various fungal species.2 Publications

Catalytic activityi

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

pH dependencei

Optimum pH is 5.5-6.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei138Proton donorIEP:1

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase B (EC:3.2.1.14)
Alternative name(s):
Chitinase B
Gene namesi
Name:chiB
ORF Names:AN4871
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome III
  • UP000005890 Componenti: Unassembled WGS sequence

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

Impairs autolysis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004298251 – 398Endochitinase BAdd BLAST398

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi66N-linked (GlcNAc...) asparagineIEP:1
Glycosylationi103N-linked (GlcNAc...) asparagineIEP:1

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

Expression is increased at the beginning of the stationary phase of growth and reaches maximum in the early autolytic phase of growth.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00005534.

Structurei

3D structure databases

ProteinModelPortaliG5EAZ3.
SMRiG5EAZ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000169884.
InParanoidiG5EAZ3.
KOiK01183.
OMAiVCYQGTW.
OrthoDBiEOG092C2AAM.

Family and domain databases

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.

G5EAZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGYKTVGYF VNWAIYGRNY NPQDLPAEKL THILYAFANV RPETGEVYLS
60 70 80 90 100
DTWSDIEKHY PTDSWNDTGN NVYGCVKQLG LLKRQHRQLK VLLSIGGWTY
110 120 130 140 150
SPNFTNGAGT PENRARFAQT ATKLITDLGF DGIDIDWEYP QNDQQAQNYV
160 170 180 190 200
DLLRRCREAL NAAQGQRRFQ LTVAVPAGPD NYNKLRLQEM TPYLDFYNLM
210 220 230 240 250
AYDYAGSWDQ TAGHQANLYP STSNPTSTPF NTVQAVNHYI DAGGVPSNKI
260 270 280 290 300
ILGMPIYGRA FQNTDGPGRP YSGIGQGTWE QGVYDYKALP RPGATEQLDT
310 320 330 340 350
NIGASWSYDP SSREMVSYDT VAAADLKAAY IQSRRLGGAM WWETSADKGG
360 370 380 390
KTANKADGSL IGTFVEDVGG VNNLDRTQNA ISYPDSQYDN LKAGFPSS
Length:398
Mass (Da):44,206
Last modified:December 14, 2011 - v1
Checksum:i216EC8D89DD48B1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BN001303 Genomic DNA. Translation: CBF76583.1.
AACD01000084 Genomic DNA. Translation: EAA60949.1.
RefSeqiXP_662475.1. XM_657383.1.

Genome annotation databases

EnsemblFungiiCADANIAT00005534; CADANIAP00005534; CADANIAG00005534.
EAA60949; EAA60949; AN4871.2.
GeneIDi2872669.
KEGGiani:AN4871.2.

Similar proteinsi

Entry informationi

Entry nameiCHIB1_EMENI
AccessioniPrimary (citable) accession number: G5EAZ3
Secondary accession number(s): C8V9U9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: December 14, 2011
Last modified: November 22, 2017
This is version 42 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

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families