ID CHIA_MAIZE Reviewed; 280 AA. AC P29022; B4FTS6; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2023, sequence version 2. DT 27-MAR-2024, entry version 143. DE RecName: Full=Endochitinase A {ECO:0000303|PubMed:1551872}; DE EC=3.2.1.14 {ECO:0000269|PubMed:1551872, ECO:0000269|PubMed:1740436, ECO:0000269|PubMed:24616181, ECO:0000269|PubMed:28328103}; DE AltName: Full=ChitA {ECO:0000303|PubMed:24616181}; DE AltName: Full=Chitinase-A {ECO:0000303|PubMed:28328103}; DE AltName: Full=Seed chitinase A {ECO:0000303|PubMed:1551872}; DE AltName: Allergen=Zea m 8 {ECO:0000305|PubMed:28328103}; DE Flags: Precursor; GN Name=CHIA {ECO:0000303|PubMed:28328103}; Synonyms=CTA1 {ECO:0000305}; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RC TISSUE=Seed; RX PubMed=1551872; DOI=10.1016/s0021-9258(19)50474-4; RA Huynh Q.K., Hironaka C.M., Levine E.B., Smith C.E., Borgmeyer J.R., RA Shah D.M.; RT "Antifungal proteins from plants. Purification, molecular cloning, and RT antifungal properties of chitinases from maize seed."; RL J. Biol. Chem. 267:6635-6640(1992). RN [2] {ECO:0000312|EMBL:ACF85519.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. B73 {ECO:0000312|EMBL:ACF85519.1}; RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740; RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J., RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J., RA Walbot V., Yu Y.; RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs."; RL PLoS Genet. 5:E1000740-E1000740(2009). RN [3] {ECO:0000312|Proteomes:UP000007305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. B73 {ECO:0000312|Proteomes:UP000007305}; RC TISSUE=Seedling {ECO:0000312|EMBL:ONM16329.1}; RG Maize Genome Sequencing Project; RA Ware D.; RT "Update maize B73 reference genome by single molecule sequencing RT technologies."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 180-195, AND ACTIVITY REGULATION. RC TISSUE=Seed; RX PubMed=1740436; DOI=10.1016/s0021-9258(19)50609-3; RA Verburg J.G., Smith C.E., Lisek C.A., Huynh Q.K.; RT "Identification of an essential tyrosine residue in the catalytic site of a RT chitinase isolated from Zea mays that is selectively modified during RT inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide."; RL J. Biol. Chem. 267:3886-3893(1992). RN [5] RP PROTEIN SEQUENCE OF 26-28 AND 47-51, FUNCTION, SIGNAL, CLEAVAGE BY RP S.MAYDIS, AND MUTAGENESIS OF ALA-47. RX PubMed=21453431; DOI=10.1111/j.1364-3703.2010.00677.x; RA Naumann T.A.; RT "Modification of recombinant maize ChitA chitinase by fungal chitinase- RT modifying proteins."; RL Mol. Plant Pathol. 12:365-372(2011). RN [6] RP FUNCTION. RX DOI=10.1016/j.pmpp.2009.10.004; RA Naumann T.A., Wickman D.T., Kendra D.F.; RT "Maize seed chitinase is modified by a protein secreted by Bipolaris RT zeicola."; RL Physiol. Mol. Plant Pathol. 74:134-141(2009). RN [7] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE BY F.VANETTENII RP EXTRACELLULAR METALLOPROTEINASE MEP. RX PubMed=24627966; DOI=10.1042/bj20140268; RA Naumann T.A., Wicklow D.T., Price N.P.; RT "Polyglycine hydrolases secreted by Pleosporineae fungi that target the RT linker region of plant class IV chitinases."; RL Biochem. J. 460:187-198(2014). RN [8] RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25966977; DOI=10.1002/pro.2705; RA Naumann T.A., Naldrett M.J., Ward T.J., Price N.P.; RT "Polyglycine hydrolases: Fungal beta-lactamase-like endoproteases that RT cleave polyglycine regions within plant class IV chitinases."; RL Protein Sci. 24:1147-1157(2015). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, AND ALLERGEN. RX PubMed=28328103; DOI=10.1111/all.13164; RA Volpicella M., Leoni C., Fanizza I., Distaso M., Leoni G., Farioli L., RA Naumann T., Pastorello E., Ceci L.R.; RT "Characterization of maize chitinase-A, a tough allergenic molecule."; RL Allergy 72:1423-1429(2017). RN [10] RP FUNCTION. RX PubMed=35240278; DOI=10.1016/j.pep.2022.106076; RA Naumann T.A., Sollenberger K.G., Hao G.; RT "Production of selenomethionine labeled polyglycine hydrolases in Pichia RT pastoris."; RL Protein Expr. Purif. 194:106076-106076(2022). RN [11] RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=36762862; DOI=10.1107/s2059798323000311; RA Dowling N.V., Naumann T.A., Price N.P.J., Rose D.R.; RT "Crystal structure of a polyglycine hydrolase determined using a RT RoseTTAFold model."; RL Acta Crystallogr. D Struct. Biol. 79:168-176(2023). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 86-278 OF MUTANT GLN-144, RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN, ACTIVE SITES, SITE, RP DISULFIDE BONDS, AND MUTAGENESIS OF GLU-144. RX PubMed=24616181; DOI=10.1002/pro.2437; RA Chaudet M.M., Naumann T.A., Price N.P., Rose D.R.; RT "Crystallographic structure of ChitA, a glycoside hydrolase family 19, RT plant class IV chitinase from Zea mays."; RL Protein Sci. 23:586-593(2014). CC -!- FUNCTION: Defense against chitin-containing fungal pathogens CC (PubMed:1551872, Ref.6). Hydrolyzes glycol chitin and tetra-N- CC acetylchitotetraose in vitro (PubMed:28328103). Its action is countered CC by fungal polyglycine hydrolases and fungalysin, that cleave the CC chitin-binding domain from the protein (PubMed:21453431, Ref.6, CC PubMed:24627966, PubMed:25966977, PubMed:35240278, PubMed:36762862). CC {ECO:0000269|PubMed:1551872, ECO:0000269|PubMed:21453431, CC ECO:0000269|PubMed:24627966, ECO:0000269|PubMed:25966977, CC ECO:0000269|PubMed:28328103, ECO:0000269|PubMed:35240278, CC ECO:0000269|PubMed:36762862, ECO:0000269|Ref.6}. 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:1551872, ECO:0000269|PubMed:1740436, CC ECO:0000269|PubMed:24616181, ECO:0000269|PubMed:28328103}; CC -!- ACTIVITY REGULATION: Inactivated by l-ethyl-3-(3- CC dimethylaminopropyl)carbodiimide (EDC) in the absence of exogenous CC nucleophiles (e.g. GlcNAc4, GlcNAc3 and GlcNAc2) (PubMed:1740436). Not CC inhibited by tetra-N-acetylchitopentaose or modified chitotetraose CC substrate TMG-chitotriomycin-pMP, containing a free, non-acetylated CC glucosaminyl residue or a N-trimethylamino glucosamine (TMG) residue at CC the non-reducing terminus, respectively (PubMed:24616181). CC {ECO:0000269|PubMed:1740436, ECO:0000269|PubMed:24616181}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.97 mM for tetra-N-acetylchitotetraose (at 37 degrees Celsius and CC pH 6) {ECO:0000269|PubMed:28328103}; CC KM=0.51 mM for tetra-N-acetylchitotetraose (at 37 degrees Celsius and CC pH 4) {ECO:0000269|PubMed:28328103}; CC KM=1.27 mM for tetra-N-acetylchitotetraose (at 50 degrees Celsius and CC pH 6) {ECO:0000269|PubMed:28328103}; CC KM=1.29 mM for tetra-N-acetylchitotetraose (at 70 degrees Celsius and CC pH 6) {ECO:0000269|PubMed:28328103}; CC Note=kcat is 56.27 sec(-1) with tetra-N-acetylchitotetraose as CC substrate (at 37 degrees Celsius and pH 6). kcat is 55.67 sec(-1) CC with tetra-N-acetylchitotetraose as substrate (at 37 degrees Celsius CC and pH 4). kcat is 69.01 sec(-1) with tetra-N-acetylchitotetraose as CC substrate (at 50 degrees Celsius and pH 6). kcat is 53.1 sec(-1) with CC tetra-N-acetylchitotetraose as substrate (at 70 degrees Celsius and CC pH 6). {ECO:0000269|PubMed:28328103}; CC pH dependence: CC Active between pH 6-3. {ECO:0000269|PubMed:28328103}; CC Temperature dependence: CC Active between 50-70 degrees Celsius. {ECO:0000269|PubMed:28328103}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28328103}. CC -!- DOMAIN: The N-terminal domain is not required for catalytic activity, CC but it is involved in substrate binding. {ECO:0000269|PubMed:24616181}. CC -!- ALLERGEN: Causes an allergic reaction in human. Food allergenic protein CC which binds IgE from sera of patients allergic to maize. CC {ECO:0000269|PubMed:28328103}. CC -!- MISCELLANEOUS: Maize chitinase B seems to be less active than chitinase CC A. {ECO:0000269|PubMed:1551872}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase CC class IV subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M84164; AAA33444.1; -; Genomic_DNA. DR EMBL; BT040514; ACF85519.1; -; mRNA. DR EMBL; BT043397; ACF88402.1; -; mRNA. DR EMBL; CM007648; ONM16329.1; -; Genomic_DNA. DR PIR; A42424; A42424. DR RefSeq; NP_001158904.1; NM_001165432.1. DR PDB; 4MCK; X-ray; 1.50 A; A=86-278. DR PDBsum; 4MCK; -. DR AlphaFoldDB; P29022; -. DR SMR; P29022; -. DR IntAct; P29022; 5. DR STRING; 4577.P29022; -. DR Allergome; 11981; Zea m 8.0101. DR Allergome; 7663; Zea m 8. DR CAZy; CBM18; Carbohydrate-Binding Module Family 18. DR CAZy; GH19; Glycoside Hydrolase Family 19. DR PaxDb; 4577-GRMZM2G051943_P01; -. DR EnsemblPlants; Zm00001eb078730_T001; Zm00001eb078730_P001; Zm00001eb078730. DR GeneID; 100283098; -. DR Gramene; Zm00001eb078730_T001; Zm00001eb078730_P001; Zm00001eb078730. DR KEGG; zma:100283098; -. DR MaizeGDB; 25130; -. DR eggNOG; KOG4742; Eukaryota. DR HOGENOM; CLU_045506_1_1_1; -. DR InParanoid; P29022; -. DR OMA; AHFTYET; -. DR OrthoDB; 997724at2759; -. DR BRENDA; 3.2.1.14; 6752. DR SABIO-RK; P29022; -. DR Proteomes; UP000007305; Chromosome 2. DR ExpressionAtlas; P29022; baseline and differential. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW. DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central. DR GO; GO:0008843; F:endochitinase activity; IDA:UniProtKB. DR GO; GO:0006040; P:amino sugar metabolic process; IDA:UniProtKB. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW. DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR CDD; cd00325; chitinase_GH19; 1. DR CDD; cd00035; ChtBD1; 1. DR Gene3D; 1.10.530.10; -; 1. DR Gene3D; 3.30.20.10; Endochitinase, domain 2; 1. DR Gene3D; 3.30.60.10; Endochitinase-like; 1. DR InterPro; IPR001002; Chitin-bd_1. DR InterPro; IPR018371; Chitin-binding_1_CS. DR InterPro; IPR036861; Endochitinase-like_sf. DR InterPro; IPR016283; Glyco_hydro_19. DR InterPro; IPR000726; Glyco_hydro_19_cat. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR PANTHER; PTHR22595; CHITINASE-RELATED; 1. DR PANTHER; PTHR22595:SF187; ENDOCHITINASE A; 1. DR Pfam; PF00187; Chitin_bind_1; 1. DR Pfam; PF00182; Glyco_hydro_19; 2. DR PIRSF; PIRSF001060; Endochitinase; 1. DR SMART; SM00270; ChtBD1; 1. DR SUPFAM; SSF53955; Lysozyme-like; 1. DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1. DR PROSITE; PS00026; CHIT_BIND_I_1; 1. DR PROSITE; PS50941; CHIT_BIND_I_2; 1. DR PROSITE; PS00773; CHITINASE_19_1; 1. DR PROSITE; PS00774; CHITINASE_19_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Carbohydrate metabolism; Chitin degradation; KW Chitin-binding; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Glycosidase; Hydrolase; Plant defense; Polysaccharide degradation; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:21453431" FT CHAIN 26..280 FT /note="Endochitinase A" FT /id="PRO_0000005303" FT DOMAIN 26..60 FT /note="Chitin-binding type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT REGION 61..77 FT /note="Hinge region (poly-Gly)" FT /evidence="ECO:0000305" FT REGION 78..280 FT /note="Catalytic" FT /evidence="ECO:0000305" FT ACT_SITE 144 FT /note="Proton donor" FT /evidence="ECO:0000305|PubMed:24616181" FT SITE 29..30 FT /note="Cleavage; by F.vanettenii Extracellular FT metalloproteinase MEP (fungalysin)" FT /evidence="ECO:0000269|PubMed:24627966" FT SITE 46..47 FT /note="Cleavage; by S.maydis" FT /evidence="ECO:0000269|PubMed:21453431" FT CARBOHYD 155 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 277 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 28..36 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 30..42 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 35..49 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 53..58 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 100..149 FT /evidence="ECO:0000269|PubMed:24616181, FT ECO:0007744|PDB:4MCK" FT DISULFID 161..170 FT /evidence="ECO:0000269|PubMed:24616181, FT ECO:0007744|PDB:4MCK" FT DISULFID 248..280 FT /evidence="ECO:0000269|PubMed:24616181, FT ECO:0007744|PDB:4MCK" FT MUTAGEN 47 FT /note="A->D: Resistance to cleavage by S.maydis." FT /evidence="ECO:0000269|PubMed:21453431" FT MUTAGEN 144 FT /note="E->Q: Loss of catalytic activity. No effect on FT substrate binding or overall structure of the catalytic FT domain." FT /evidence="ECO:0000269|PubMed:24616181" FT CONFLICT 229 FT /note="R -> G (in Ref. 1; AAA33444)" FT /evidence="ECO:0000305" FT CONFLICT 279 FT /note="T -> I (in Ref. 1; AAA33444)" FT /evidence="ECO:0000305" FT HELIX 86..93 FT /evidence="ECO:0007829|PDB:4MCK" FT TURN 101..105 FT /evidence="ECO:0007829|PDB:4MCK" FT HELIX 108..115 FT /evidence="ECO:0007829|PDB:4MCK" FT TURN 119..122 FT /evidence="ECO:0007829|PDB:4MCK" FT HELIX 127..145 FT /evidence="ECO:0007829|PDB:4MCK" FT TURN 146..149 FT /evidence="ECO:0007829|PDB:4MCK" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:4MCK" FT TURN 180..183 FT /evidence="ECO:0007829|PDB:4MCK" FT HELIX 187..197 FT /evidence="ECO:0007829|PDB:4MCK" FT TURN 201..203 FT /evidence="ECO:0007829|PDB:4MCK" FT HELIX 207..210 FT /evidence="ECO:0007829|PDB:4MCK" FT HELIX 212..226 FT /evidence="ECO:0007829|PDB:4MCK" FT HELIX 228..233 FT /evidence="ECO:0007829|PDB:4MCK" FT HELIX 235..242 FT /evidence="ECO:0007829|PDB:4MCK" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:4MCK" FT HELIX 253..269 FT /evidence="ECO:0007829|PDB:4MCK" SQ SEQUENCE 280 AA; 29212 MW; 4FD44B67238C0671 CRC64; MANAPRILAL GLLALLCAAA GPAAAQNCGC QPNFCCSKFG YCGTTDAYCG DGCQSGPCRS GGGGGGGGGG GGGGSGGANV ANVVTDAFFN GIKNQAGSGC EGKNFYTRSA FLSAVNAYPG FAHGGTEVEG KREIAAFFAH VTHETGHFCY ISEINKSNAY CDASNRQWPC AAGQKYYGRG PLQISWNYNY GPAGRDIGFN GLADPNRVAQ DAVIAFKTAL WFWMNNVHRV MPQGFGATIR AINGALECNG NNPAQMNARV GYYKQYCQQL RVDPGPNLTC //