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Endochitinase A1 (EC 3.2.1.14) (Chitinase A1)

 CHIA1_ASPFM             Reviewed;         825 AA.
Q873Y0;
09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
12-SEP-2018, entry version 71.
RecName: Full=Endochitinase A1;
EC=3.2.1.14;
AltName: Full=Chitinase A1;
Flags: Precursor;
Name=chiA1; Synonyms=chi1;
Neosartorya fumigata (Aspergillus fumigatus).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=746128;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NIH 5233 / ATCC 13073;
PubMed=14523125; DOI=10.1099/mic.0.26476-0;
Jaques A.K., Fukamizo T., Hall D., Barton R.C., Escott G.M.,
Parkinson T., Hitchcock C.A., Adams D.J.;
"Disruption of the gene encoding the ChiB1 chitinase of Aspergillus
fumigatus and characterization of a recombinant gene product.";
Microbiology 149:2931-2939(2003).
[2]
INDUCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
PubMed=16096835; DOI=10.1007/s00203-005-0028-x;
Taib M., Pinney J.W., Westhead D.R., McDowall K.J., Adams D.J.;
"Differential expression and extent of fungal/plant and
fungal/bacterial chitinases of Aspergillus fumigatus.";
Arch. Microbiol. 184:78-81(2005).
[3]
GLYCOSYLATION.
PubMed=20398215; DOI=10.1111/j.1365-2958.2010.07164.x;
Mouyna I., Kniemeyer O., Jank T., Loussert C., Mellado E.,
Aimanianda V., Beauvais A., Wartenberg D., Sarfati J., Bayry J.,
Prevost M.C., Brakhage A.A., Strahl S., Huerre M., Latge J.P.;
"Members of protein O-mannosyltransferase family in Aspergillus
fumigatus differentially affect growth, morphogenesis and viability.";
Mol. Microbiol. 76:1205-1221(2010).
[4]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=20974863; DOI=10.1128/AAC.00884-10;
Cagas S.E., Jain M.R., Li H., Perlin D.S.;
"Profiling the Aspergillus fumigatus proteome in response to
caspofungin.";
Antimicrob. Agents Chemother. 55:146-154(2011).
[5]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 29-337 IN COMPLEX WITH
INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND ACTIVITY REGULATION.
PubMed=21168763; DOI=10.1016/j.chembiol.2010.07.018;
Rush C.L., Schuttelkopf A.W., Hurtado-Guerrero R., Blair D.E.,
Ibrahim A.F., Desvergnes S., Eggleston I.M., van Aalten D.M.;
"Natural product-guided discovery of a fungal chitinase inhibitor.";
Chem. Biol. 17:1275-1281(2010).
-!- FUNCTION: GPI-anchored 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).
Required to reshape the cell wall at the sites where cell wall
remodeling and/or cell wall maturation actively take place such as
sites of conidia formation. {ECO:0000269|PubMed:21168763}.
-!- CATALYTIC ACTIVITY: Random endo-hydrolysis of N-acetyl-beta-D-
glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
{ECO:0000269|PubMed:16096835, ECO:0000269|PubMed:21168763}.
-!- ACTIVITY REGULATION: The cyclic peptide natural product argifin
acts as a specific inhibitor. {ECO:0000269|PubMed:21168763}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=300 uM for 4-methylumbelliferyl beta-D-N,N'-
diacetylchitobiose {ECO:0000269|PubMed:21168763};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}. Secreted, cell wall
{ECO:0000269|PubMed:16096835, ECO:0000269|PubMed:20974863}.
-!- INDUCTION: Shows high levels of constitutive expression and
repressed by caspofungin. {ECO:0000269|PubMed:16096835,
ECO:0000269|PubMed:20974863}.
-!- PTM: O-mannosylated by pmt4.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
class III subfamily. {ECO:0000305}.
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EMBL; AY217659; AAO61685.1; -; Genomic_DNA.
PDB; 2XUC; X-ray; 2.30 A; A/B/C=29-337.
PDB; 2XVN; X-ray; 2.35 A; A/B/C=29-337.
PDBsum; 2XUC; -.
PDBsum; 2XVN; -.
ProteinModelPortal; Q873Y0; -.
SMR; Q873Y0; -.
BindingDB; Q873Y0; -.
ChEMBL; CHEMBL1293196; -.
CAZy; GH18; Glycoside Hydrolase Family 18.
EvolutionaryTrace; Q873Y0; -.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
InterPro; IPR001223; Glyco_hydro18_cat.
InterPro; IPR001579; Glyco_hydro_18_chit_AS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00704; Glyco_hydro_18; 1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS01095; CHITINASE_18; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Cell membrane; Cell wall;
Chitin degradation; Chitin-binding; Glycoprotein; Glycosidase;
GPI-anchor; Hydrolase; Lipoprotein; Membrane;
Polysaccharide degradation; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 800 Endochitinase A1.
/FTId=PRO_0000429814.
PROPEP 801 825 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000429815.
REGION 170 174 Inhibitor binding.
REGION 230 232 Inhibitor binding.
COMPBIAS 346 689 Ser/Thr-rich.
ACT_SITE 174 174 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10053}.
BINDING 34 34 Inhibitor. {ECO:0000269|PubMed:21168763}.
BINDING 124 124 Inhibitor; via amide nitrogen.
{ECO:0000269|PubMed:21168763}.
BINDING 125 125 Inhibitor. {ECO:0000269|PubMed:21168763}.
BINDING 207 207 Inhibitor. {ECO:0000269|PubMed:21168763}.
BINDING 312 312 Inhibitor. {ECO:0000269|PubMed:21168763}.
LIPID 800 800 GPI-anchor amidated glycine.
{ECO:0000255}.
CARBOHYD 559 559 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 717 717 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
STRAND 30 36 {ECO:0000244|PDB:2XUC}.
HELIX 44 48 {ECO:0000244|PDB:2XUC}.
STRAND 55 61 {ECO:0000244|PDB:2XUC}.
HELIX 65 67 {ECO:0000244|PDB:2XUC}.
HELIX 69 71 {ECO:0000244|PDB:2XUC}.
HELIX 78 80 {ECO:0000244|PDB:2XUC}.
STRAND 85 87 {ECO:0000244|PDB:2XUC}.
STRAND 93 97 {ECO:0000244|PDB:2XUC}.
HELIX 101 112 {ECO:0000244|PDB:2XUC}.
STRAND 116 127 {ECO:0000244|PDB:2XUC}.
HELIX 134 148 {ECO:0000244|PDB:2XUC}.
TURN 160 163 {ECO:0000244|PDB:2XUC}.
STRAND 167 173 {ECO:0000244|PDB:2XUC}.
HELIX 181 193 {ECO:0000244|PDB:2XUC}.
STRAND 201 204 {ECO:0000244|PDB:2XUC}.
STRAND 207 211 {ECO:0000244|PDB:2XUC}.
TURN 213 215 {ECO:0000244|PDB:2XUC}.
HELIX 216 221 {ECO:0000244|PDB:2XUC}.
STRAND 225 230 {ECO:0000244|PDB:2XUC}.
HELIX 235 237 {ECO:0000244|PDB:2XUC}.
HELIX 240 242 {ECO:0000244|PDB:2XUC}.
HELIX 252 260 {ECO:0000244|PDB:2XUC}.
TURN 263 266 {ECO:0000244|PDB:2XUC}.
STRAND 268 276 {ECO:0000244|PDB:2XUC}.
HELIX 277 279 {ECO:0000244|PDB:2XUC}.
HELIX 288 301 {ECO:0000244|PDB:2XUC}.
TURN 303 305 {ECO:0000244|PDB:2XUC}.
STRAND 306 312 {ECO:0000244|PDB:2XUC}.
HELIX 314 319 {ECO:0000244|PDB:2XUC}.
HELIX 327 336 {ECO:0000244|PDB:2XUC}.
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


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