CHIB1_EMENI
ID CHIB1_EMENI Reviewed; 398 AA.
AC G5EAZ3; C8V9U9;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Endochitinase B;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase B;
GN Name=chiB; ORFNames=AN4871;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18800599; DOI=10.1556/amicr.55.2008.3.6;
RA Erdei E., Pusztahelyi T., Miskei M., Barna T., Pocsi I.;
RT "Characterization and heterologous expression of an age-dependent
RT fungal/bacterial type chitinase of Aspergillus nidulans.";
RL Acta Microbiol. Immunol. Hung. 55:351-361(2008).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION.
RX PubMed=19486415; DOI=10.1111/j.1365-2672.2009.04237.x;
RA Pocsi I., Leiter E., Kwon N.J., Shin K.S., Kwon G.S., Pusztahelyi T.,
RA Emri T., Abuknesha R.A., Price R.G., Yu J.H.;
RT "Asexual sporulation signalling regulates autolysis of Aspergillus nidulans
RT via modulating the chitinase ChiB production.";
RL J. Appl. Microbiol. 107:514-523(2009).
RN [5]
RP FUNCTION.
RX PubMed=23124755; DOI=10.1007/s12275-012-2001-0;
RA Szilagyi M., Anton F., Forgacs K., Yu J.H., Pocsi I., Emri T.;
RT "Antifungal activity of extracellular hydrolases produced by autolysing
RT Aspergillus nidulans cultures.";
RL J. Microbiol. 50:849-854(2012).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=25043916; DOI=10.1186/1471-2164-15-613;
RA Martins I., Hartmann D.O., Alves P.C., Martins C., Garcia H.,
RA Leclercq C.C., Ferreira R., He J., Renaut J., Becker J.D.,
RA Silva Pereira C.;
RT "Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant
RT polyester suberin as carbon source.";
RL BMC Genomics 15:613-613(2014).
CC -!- FUNCTION: Major secreted chitinase involved in the degradation of
CC chitin, a component of the cell walls of fungi and exoskeletal elements
CC of some animals (including worms and arthropods). Plays a role in the
CC morphogenesis and autolysis. Has also significant antifungal activity
CC against various fungal species. {ECO:0000269|PubMed:19486415,
CC ECO:0000269|PubMed:23124755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000269|PubMed:18800599};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5-6.5. {ECO:0000269|PubMed:18800599};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25043916}.
CC -!- INDUCTION: Expression is increased at the beginning of the stationary
CC phase of growth and reaches maximum in the early autolytic phase of
CC growth. {ECO:0000269|PubMed:19486415}.
CC -!- DISRUPTION PHENOTYPE: Impairs autolysis. {ECO:0000269|PubMed:19486415}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; BN001303; CBF76583.1; -; Genomic_DNA.
DR EMBL; AACD01000084; EAA60949.1; -; Genomic_DNA.
DR RefSeq; XP_662475.1; XM_657383.1.
DR AlphaFoldDB; G5EAZ3; -.
DR SMR; G5EAZ3; -.
DR STRING; 162425.CADANIAP00005534; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EnsemblFungi; CBF76583; CBF76583; ANIA_04871.
DR EnsemblFungi; EAA60949; EAA60949; AN4871.2.
DR GeneID; 2872669; -.
DR KEGG; ani:AN4871.2; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_1_0_1; -.
DR InParanoid; G5EAZ3; -.
DR OMA; NPMTYDF; -.
DR OrthoDB; 1289629at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted.
FT CHAIN 1..398
FT /note="Endochitinase B"
FT /id="PRO_0000429825"
FT DOMAIN 4..363
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 69..70
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 96..99
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 139
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 200..203
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 342
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 398 AA; 44206 MW; 216EC8D89DD48B1B CRC64;
MSGYKTVGYF VNWAIYGRNY NPQDLPAEKL THILYAFANV RPETGEVYLS DTWSDIEKHY
PTDSWNDTGN NVYGCVKQLG LLKRQHRQLK VLLSIGGWTY SPNFTNGAGT PENRARFAQT
ATKLITDLGF DGIDIDWEYP QNDQQAQNYV DLLRRCREAL NAAQGQRRFQ LTVAVPAGPD
NYNKLRLQEM TPYLDFYNLM AYDYAGSWDQ TAGHQANLYP STSNPTSTPF NTVQAVNHYI
DAGGVPSNKI ILGMPIYGRA FQNTDGPGRP YSGIGQGTWE QGVYDYKALP RPGATEQLDT
NIGASWSYDP SSREMVSYDT VAAADLKAAY IQSRRLGGAM WWETSADKGG KTANKADGSL
IGTFVEDVGG VNNLDRTQNA ISYPDSQYDN LKAGFPSS
