CHIA1_ASPFM
ID CHIA1_ASPFM Reviewed; 825 AA.
AC Q873Y0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Endochitinase A1;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase A1;
DE Flags: Precursor;
GN Name=chiA1; Synonyms=chi1;
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].
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 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 [3]
RP GLYCOSYLATION.
RX PubMed=20398215; DOI=10.1111/j.1365-2958.2010.07164.x;
RA Mouyna I., Kniemeyer O., Jank T., Loussert C., Mellado E., Aimanianda V.,
RA Beauvais A., Wartenberg D., Sarfati J., Bayry J., Prevost M.C.,
RA Brakhage A.A., Strahl S., Huerre M., Latge J.P.;
RT "Members of protein O-mannosyltransferase family in Aspergillus fumigatus
RT differentially affect growth, morphogenesis and viability.";
RL Mol. Microbiol. 76:1205-1221(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=20974863; DOI=10.1128/aac.00884-10;
RA Cagas S.E., Jain M.R., Li H., Perlin D.S.;
RT "Profiling the Aspergillus fumigatus proteome in response to caspofungin.";
RL Antimicrob. Agents Chemother. 55:146-154(2011).
RN [5] {ECO:0007744|PDB:2XUC, ECO:0007744|PDB:2XVN}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 29-337 IN COMPLEX WITH INHIBITOR,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=21168763; DOI=10.1016/j.chembiol.2010.07.018;
RA Rush C.L., Schuttelkopf A.W., Hurtado-Guerrero R., Blair D.E.,
RA Ibrahim A.F., Desvergnes S., Eggleston I.M., van Aalten D.M.;
RT "Natural product-guided discovery of a fungal chitinase inhibitor.";
RL Chem. Biol. 17:1275-1281(2010).
CC -!- FUNCTION: GPI-anchored chitinase involved in the degradation of chitin,
CC a component of the cell walls of fungi and exoskeletal elements of some
CC animals (including worms and arthropods). Required to reshape the cell
CC wall at the sites where cell wall remodeling and/or cell wall
CC maturation actively take place such as sites of conidia formation.
CC {ECO:0000269|PubMed:21168763}.
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:16096835, ECO:0000269|PubMed:21168763};
CC -!- ACTIVITY REGULATION: The cyclic peptide natural product argifin acts as
CC a specific inhibitor. {ECO:0000269|PubMed:21168763}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=300 uM for 4-methylumbelliferyl beta-D-N,N'-diacetylchitobiose
CC {ECO:0000269|PubMed:21168763};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Secreted, cell wall {ECO:0000269|PubMed:16096835,
CC ECO:0000269|PubMed:20974863}.
CC -!- INDUCTION: Shows high levels of constitutive expression and repressed
CC by caspofungin. {ECO:0000269|PubMed:16096835,
CC ECO:0000269|PubMed:20974863}.
CC -!- PTM: O-mannosylated by pmt4.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
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DR EMBL; AY217659; AAO61685.1; -; Genomic_DNA.
DR PDB; 2XUC; X-ray; 2.30 A; A/B/C=29-337.
DR PDB; 2XVN; X-ray; 2.35 A; A/B/C=29-337.
DR PDBsum; 2XUC; -.
DR PDBsum; 2XVN; -.
DR AlphaFoldDB; Q873Y0; -.
DR SMR; Q873Y0; -.
DR BindingDB; Q873Y0; -.
DR ChEMBL; CHEMBL1293196; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PRIDE; Q873Y0; -.
DR SABIO-RK; Q873Y0; -.
DR EvolutionaryTrace; Q873Y0; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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 CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR045321; Cts1-like.
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 SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell membrane; Cell wall;
KW Chitin degradation; Chitin-binding; Glycoprotein; Glycosidase; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Polysaccharide degradation; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..800
FT /note="Endochitinase A1"
FT /id="PRO_0000429814"
FT PROPEP 801..825
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429815"
FT DOMAIN 29..338
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 338..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT LIPID 800
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:2XUC"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2XUC"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2XUC"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:2XUC"
FT STRAND 116..127
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:2XUC"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:2XUC"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:2XUC"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2XUC"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:2XUC"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:2XUC"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:2XUC"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:2XUC"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:2XUC"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2XUC"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:2XUC"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:2XUC"
SQ SEQUENCE 825 AA; 83088 MW; 8C2017A8FD1A208C CRC64;
MVSSKLSFVA TAVAALAPLA SAFDASSRSN LAIYWGQGPN QLRLSHFCQE TSLDIINIGF
INYFPDMSPG HWPGSNFGNQ CDGSVYVTND GVVTKLLSGC HQIMEDIPIC QAAGKKVLLS
IGGAYPPDQS ILSEDSAVAF ATFLWGAFGP VAEGWEGPRP FGDVVVDGFD FDIEHNGGFG
YATMVNTFRQ YFNQVPERKF YLSAAPQCII PDAQLSDAIF NAAFDFIWIQ YYNTAACSAK
SFIDTSLGTF NFDAWVTVLK ASASKDAKLY VGLPASETAA NQGYYLTPDE VESLVSTYMD
RYPDTFGGIM LWEATASENN QIDGAPYADH MKDILLHCDP SPPVTSSSAV PSSTPVTTPS
PSSSAVPSST PAVSETPSPS SSAVPSSTPV ASSTPVVPGT SASSSPVSSS SAIAPSTPVV
PGTSTPSSTP VASSTPVVPG TSASSSPVSS SSAVASSTPV VPGTSVPSST PAIPGGSSSS
SEAVASSTPL VTLTLTVSPT PAPSSSESSS TDLSSSTQTD VGTAPSQPAG PSTTATATTS
SSSSSTDESS TTVGSGNGNG SGSTTTTAAT DSITAAPTAT SSATATGATS EPVTITTIIV
TSYIDICPTG FTTVTTTYTT TYCPGTNTAT ATATVTNPPS GPGGAGSQTT APTVPEGWTT
TVTVCTQCAA KPTTVTLTLP VTETGSTSTD AVPAPPAATG EGSNPTQPSG ASPTGGNGSF
SEEPVPPPAV TQVSTSTEIV TLVRPTSSRP LILGTGTVHP SSTLAVKPSA KPSGQNSGSS
SHVPIPPSYT QEAVSPLSTG AASRVTGLGH GLVLTVLTLS AFFVL
