CHI4_CANAL
ID CHI4_CANAL Reviewed; 388 AA.
AC Q5AM60; A0A1D8PGH9; Q5ALR1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Chitinase 4;
DE EC=3.2.1.14;
GN Name=CHT4; OrderedLocusNames=CAALFM_C202010CA;
GN ORFNames=CaO19.1515, CaO19.9090;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=18809304; DOI=10.1016/j.micres.2008.08.005;
RA Dunkler A., Jorde S., Wendland J.;
RT "An Ashbya gossypii cts2 mutant deficient in a sporulation-specific
RT chitinase can be complemented by Candida albicans CHT4.";
RL Microbiol. Res. 163:701-710(2008).
CC -!- FUNCTION: Chitinase involved in the remodeling of chitin in the fungal
CC cell wall. Plays a role in sporulation. {ECO:0000269|PubMed:18809304}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; CP017624; AOW27242.1; -; Genomic_DNA.
DR RefSeq; XP_722560.1; XM_717467.1.
DR AlphaFoldDB; Q5AM60; -.
DR SMR; Q5AM60; -.
DR BioGRID; 1218862; 1.
DR STRING; 237561.Q5AM60; -.
DR PRIDE; Q5AM60; -.
DR GeneID; 3635768; -.
DR KEGG; cal:CAALFM_C202010CA; -.
DR CGD; CAL0000185677; CHT4.
DR VEuPathDB; FungiDB:C2_02010C_A; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_1_0_1; -.
DR OrthoDB; 1289629at2759; -.
DR PRO; PR:Q5AM60; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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 GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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 PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Sporulation.
FT CHAIN 1..388
FT /note="Chitinase 4"
FT /id="PRO_0000429925"
FT DOMAIN 22..375
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 82..83
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 109..112
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 152
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 208..211
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 350
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 388 AA; 44360 MW; CB89FCD516D35E0B CRC64;
MCHKMMNKFQ QRLHHTTSTP LFKTCVYFSN WSVYQKKHFP QDIPIEYYTH IFYAFILIDE
QTGKLKFSDE WCDLQMPQPS PNQSITGNLQ QFYEMKKKNR HLKLIMSIGG WGTCHLFESV
VSNDTKFDNF VNSTIEFAEK YGFDGVDIDW EYPKNSTQAA KLVELLARLR NKLNSKYIIT
VAAPGGSDNI EILKIQEMDK YLTFWNLMCY DFAGEGWSSK TAFHSNLFGN NGDNSLNASD
VVQTYINKGV HPTKLILGMP MYGRIFHGVD RPEIGIPFTK ERKSGCIEAD VVDYNKFGDT
FDYEDFDPRK VGALKYDSHS KQLITFDNLQ CARIKASFIQ SRQLGGGMWW DSAGDVSVTN
DGCLVKNFVD QLGGVEVLEK SANNLHGC
