CHIB1_ASPFM
ID CHIB1_ASPFM Reviewed; 433 AA.
AC Q873X9; Q4WB85;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Endochitinase B1;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase B1;
DE Flags: Precursor;
GN Name=chiB1;
OS Neosartorya fumigata (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=746128;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, GLYCOSYLATION,
RP CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=NIH 5233 / ATCC 13073;
RX PubMed=14523125; DOI=10.1099/mic.0.26476-0;
RA Jaques A.K., Fukamizo T., Hall D., Barton R.C., Escott G.M., Parkinson T.,
RA Hitchcock C.A., Adams D.J.;
RT "Disruption of the gene encoding the ChiB1 chitinase of Aspergillus
RT fumigatus and characterization of a recombinant gene product.";
RL Microbiology 149:2931-2939(2003).
RN [2]
RP CRYSTALLIZATION.
RX PubMed=15103145; DOI=10.1107/s0907444904005190;
RA Hu H., Wang G., Yang H., Zhou J., Mo L., Yang K., Jin C., Jin C., Rao Z.;
RT "Crystallization and preliminary crystallographic analysis of a native
RT chitinase from the fungal pathogen Aspergillus fumigatus YJ-407.";
RL Acta Crystallogr. D 60:939-940(2004).
RN [3]
RP INDUCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=16096835; DOI=10.1007/s00203-005-0028-x;
RA Taib M., Pinney J.W., Westhead D.R., McDowall K.J., Adams D.J.;
RT "Differential expression and extent of fungal/plant and fungal/bacterial
RT chitinases of Aspergillus fumigatus.";
RL Arch. Microbiol. 184:78-81(2005).
RN [4]
RP MUTAGENESIS OF TRP-137; MET-243 AND ASP-246, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18975073; DOI=10.1007/s10719-008-9203-z;
RA Lu Y., Yang H., Hu H., Wang Y., Rao Z., Jin C.;
RT "Mutation of Trp137 to glutamate completely removes transglycosyl activity
RT associated with the Aspergillus fumigatus AfChiB1.";
RL Glycoconj. J. 26:525-534(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 39-433 IN COMPLEX WITH INHIBITOR.
RA Hu H., Wang G., Yang H., Zhou J., Mo L., Yang K., Jin C., Jin C., Rao Z.;
RT "Crystal structure of a native chitinase from Aspergillus fumigatus YJ-
RT 407.";
RL Submitted (AUG-2004) to the PDB data bank.
RN [6] {ECO:0007744|PDB:1W9P, ECO:0007744|PDB:1W9U, ECO:0007744|PDB:1W9V}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH INHIBITOR, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-137; THR-138;
RP ASP-175; GLU-177; ALA-217; MET-243; TYR-245; ASP-246; PHE-251; ARG-301 AND
RP GLU-322, AND ACTIVITY REGULATION.
RX PubMed=15664516; DOI=10.1016/j.chembiol.2004.10.013;
RA Rao F.V., Houston D.R., Boot R.G., Aerts J.M., Hodkinson M., Adams D.J.,
RA Shiomi K., Omura S., van Aalten D.M.;
RT "Specificity and affinity of natural product cyclopentapeptide inhibitors
RT against A. fumigatus, human, and bacterial chitinases.";
RL Chem. Biol. 12:65-76(2005).
RN [7] {ECO:0007744|PDB:2A3A, ECO:0007744|PDB:2A3B, ECO:0007744|PDB:2A3C, ECO:0007744|PDB:2A3E}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF TRP-137; THR-138; ASP-175; GLU-177; ALA-217;
RP MET-243; TYR-245; ASP-246; ARG-301 AND GLU-322, AND ACTIVITY REGULATION.
RX PubMed=16183021; DOI=10.1016/j.chembiol.2005.07.009;
RA Rao F.V., Andersen O.A., Vora K.A., Demartino J.A., van Aalten D.M.;
RT "Methylxanthine drugs are chitinase inhibitors: investigation of inhibition
RT and binding modes.";
RL Chem. Biol. 12:973-980(2005).
RN [8] {ECO:0007744|PDB:2IUZ}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH INHIBITOR, AND
RP ACTIVITY REGULATION.
RX PubMed=16844689; DOI=10.1074/jbc.m604048200;
RA Schuttelkopf A.W., Andersen O.A., Rao F.V., Allwood M., Lloyd C.,
RA Eggleston I.M., van Aalten D.M.;
RT "Screening-based discovery and structural dissection of a novel family 18
RT chitinase inhibitor.";
RL J. Biol. Chem. 281:27278-27285(2006).
RN [9] {ECO:0007744|PDB:2IUZ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR, AND
RP ACTIVITY REGULATION.
RX PubMed=18355729; DOI=10.1016/j.chembiol.2008.02.015;
RA Andersen O.A., Nathubhai A., Dixon M.J., Eggleston I.M., van Aalten D.M.;
RT "Structure-based dissection of the natural product cyclopentapeptide
RT chitinase inhibitor argifin.";
RL Chem. Biol. 15:295-301(2008).
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 (By similarity). {ECO:0000250}.
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:14523125, ECO:0000269|PubMed:15664516,
CC ECO:0000269|PubMed:16096835, ECO:0000269|PubMed:16183021,
CC ECO:0000269|PubMed:18975073};
CC -!- ACTIVITY REGULATION: Methylxanthine drugs surch as theophylline,
CC caffeine and pentoxifylline, as well as the two cyclic peptide natural
CC products argifin and argadin, act as specific inhibitors.
CC {ECO:0000269|PubMed:15664516, ECO:0000269|PubMed:16183021,
CC ECO:0000269|PubMed:16844689, ECO:0000269|PubMed:18355729}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.9 uM for 4-methylumbelliferyl beta-D-N,N'-diacetylchitobiose
CC {ECO:0000269|PubMed:15664516, ECO:0000269|PubMed:18975073};
CC KM=2.94 mg/ml for chitosan {ECO:0000269|PubMed:15664516,
CC ECO:0000269|PubMed:18975073};
CC pH dependence:
CC Optimum pH is 5.0-7.0. {ECO:0000269|PubMed:15664516,
CC ECO:0000269|PubMed:18975073};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:15664516, ECO:0000269|PubMed:18975073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14523125,
CC ECO:0000269|PubMed:16096835}.
CC -!- INDUCTION: Induced during batch culture. {ECO:0000269|PubMed:16096835}.
CC -!- DISRUPTION PHENOTYPE: Decreases the level of chitinase activity during
CC the autolytic phase of batch cultures. {ECO:0000269|PubMed:14523125}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; AY217660; AAO61686.1; -; Genomic_DNA.
DR PDB; 1W9P; X-ray; 1.70 A; A/B=1-433.
DR PDB; 1W9U; X-ray; 1.85 A; A/B=1-433.
DR PDB; 1W9V; X-ray; 2.00 A; A/B=1-433.
DR PDB; 1WNO; X-ray; 2.10 A; A/B=39-433.
DR PDB; 2A3A; X-ray; 2.10 A; A/B=1-433.
DR PDB; 2A3B; X-ray; 1.90 A; A/B=1-433.
DR PDB; 2A3C; X-ray; 2.07 A; A/B=1-433.
DR PDB; 2A3E; X-ray; 1.95 A; A/B=1-433.
DR PDB; 2IUZ; X-ray; 1.95 A; A/B=1-433.
DR PDB; 3CH9; X-ray; 2.20 A; A/B=1-433.
DR PDB; 3CHC; X-ray; 1.90 A; A/B=1-433.
DR PDB; 3CHD; X-ray; 2.00 A; A/B=1-433.
DR PDB; 3CHE; X-ray; 2.05 A; A/B=1-433.
DR PDB; 3CHF; X-ray; 1.95 A; A/B=1-433.
DR PDBsum; 1W9P; -.
DR PDBsum; 1W9U; -.
DR PDBsum; 1W9V; -.
DR PDBsum; 1WNO; -.
DR PDBsum; 2A3A; -.
DR PDBsum; 2A3B; -.
DR PDBsum; 2A3C; -.
DR PDBsum; 2A3E; -.
DR PDBsum; 2IUZ; -.
DR PDBsum; 3CH9; -.
DR PDBsum; 3CHC; -.
DR PDBsum; 3CHD; -.
DR PDBsum; 3CHE; -.
DR PDBsum; 3CHF; -.
DR AlphaFoldDB; Q873X9; -.
DR SMR; Q873X9; -.
DR BindingDB; Q873X9; -.
DR ChEMBL; CHEMBL4638; -.
DR DrugBank; DB04350; Argadin.
DR DrugBank; DB03632; Argifin.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18A_ASPFU; -.
DR OMA; FYYCSGG; -.
DR EvolutionaryTrace; Q873X9; -.
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 3D-structure; Carbohydrate metabolism; Chitin degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..433
FT /note="Endochitinase B1"
FT /id="PRO_0000429823"
FT DOMAIN 43..407
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 177
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 52
FT /ligand="caffeine"
FT /ligand_id="ChEBI:CHEBI:27732"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16183021,
FT ECO:0007744|PDB:2A3B"
FT BINDING 108..109
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 135..138
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 137
FT /ligand="caffeine"
FT /ligand_id="ChEBI:CHEBI:27732"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16183021,
FT ECO:0007744|PDB:2A3B"
FT BINDING 178
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 243..246
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 245
FT /ligand="caffeine"
FT /ligand_id="ChEBI:CHEBI:27732"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16183021,
FT ECO:0007744|PDB:2A3B"
FT BINDING 251
FT /ligand="caffeine"
FT /ligand_id="ChEBI:CHEBI:27732"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16183021,
FT ECO:0007744|PDB:2A3B"
FT BINDING 384
FT /ligand="caffeine"
FT /ligand_id="ChEBI:CHEBI:27732"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16183021,
FT ECO:0007744|PDB:2A3B"
FT BINDING 384
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 137
FT /note="W->A: Affects substrate-binding and completely
FT abrogates argifin/argadin-binding."
FT /evidence="ECO:0000269|PubMed:15664516,
FT ECO:0000269|PubMed:16183021, ECO:0000269|PubMed:18975073"
FT MUTAGEN 138
FT /note="T->A: Affects binding to argifin and argadin."
FT /evidence="ECO:0000269|PubMed:15664516,
FT ECO:0000269|PubMed:16183021"
FT MUTAGEN 175
FT /note="D->A: Impairs catalytic activity and decreases
FT argifin/argadin-binding but not substrate-binding."
FT /evidence="ECO:0000269|PubMed:15664516,
FT ECO:0000269|PubMed:16183021"
FT MUTAGEN 177
FT /note="E->A: Impairs catalytic activity and decreases
FT argifin/argadin-binding but not substrate-binding."
FT /evidence="ECO:0000269|PubMed:15664516,
FT ECO:0000269|PubMed:16183021"
FT MUTAGEN 217
FT /note="A->G: Affects binding to argifin."
FT /evidence="ECO:0000269|PubMed:15664516,
FT ECO:0000269|PubMed:16183021"
FT MUTAGEN 243
FT /note="M->A: Affects binding to argadin."
FT /evidence="ECO:0000269|PubMed:15664516,
FT ECO:0000269|PubMed:16183021, ECO:0000269|PubMed:18975073"
FT MUTAGEN 245
FT /note="Y->F: Impairs catalytic activity and decreases
FT argifin/argadin-binding but not substrate-binding."
FT /evidence="ECO:0000269|PubMed:15664516,
FT ECO:0000269|PubMed:16183021"
FT MUTAGEN 246
FT /note="D->A: Impairs catalytic activity and decreases
FT argifin/argadin-binding but not substrate-binding."
FT /evidence="ECO:0000269|PubMed:15664516,
FT ECO:0000269|PubMed:16183021, ECO:0000269|PubMed:18975073"
FT MUTAGEN 251
FT /note="F->A: Affects substrate-binding and completely
FT abrogates argifin/argadin-binding."
FT /evidence="ECO:0000269|PubMed:15664516"
FT MUTAGEN 301
FT /note="R->K: Impairs catalytic activity but not substrate-
FT binding."
FT /evidence="ECO:0000269|PubMed:15664516,
FT ECO:0000269|PubMed:16183021"
FT MUTAGEN 322
FT /note="E->A: Affects binding to argifin and argadin."
FT /evidence="ECO:0000269|PubMed:15664516,
FT ECO:0000269|PubMed:16183021"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:1W9P"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1W9P"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 150..167
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 182..206
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1WNO"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:1W9U"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 292..305
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:1W9P"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 363..376
FT /evidence="ECO:0007829|PDB:1W9P"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:1W9P"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:1W9P"
SQ SEQUENCE 433 AA; 47622 MW; 95AECA3DCE917D30 CRC64;
MRFATSTIVK VALLLSSLCV DAAVMWNRDT SSTDLEARAS SGYRSVVYFV NWAIYGRNHN
PQDLPVERLT HVLYAFANVR PETGEVYMTD SWADIEKHYP GDSWSDTGNN VYGCIKQLYL
LKKQNRNLKV LLSIGGWTYS PNFAPAASTD AGRKNFAKTA VKLLQDLGFD GLDIDWEYPE
NDQQANDFVL LLKEVRTALD SYSAANAGGQ HFLLTVASPA GPDKIKVLHL KDMDQQLDFW
NLMAYDYAGS FSSLSGHQAN VYNDTSNPLS TPFNTQTALD LYRAGGVPAN KIVLGMPLYG
RSFANTDGPG KPYNGVGQGS WENGVWDYKA LPQAGATEHV LPDIMASYSY DATNKFLISY
DNPQVANLKS GYIKSLGLGG AMWWDSSSDK TGSDSLITTV VNALGGTGVF EQSQNELDYP
VSQYDNLRNG MQT
