ID   CHIB_MAIZE              Reviewed;         269 AA.
AC   P29023;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-NOV-2008, entry version 63.
DE   RecName: Full=Endochitinase B;
DE            EC=3.2.1.14;
DE   AltName: Full=Seed chitinase B;
DE   Flags: Precursor; Fragment;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACCAD clade; Panicoideae; Andropogoneae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Seed;
RX   MEDLINE=92202208; PubMed=1551872;
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]
RP   PROTEIN SEQUENCE OF 169-184.
RC   TISSUE=Seed;
RX   MEDLINE=92156129; PubMed=1740436;
RA   Verburg J.G., Smith C.E., Lisek C.A., Huynh Q.K.;
RT   "Identification of an essential tyrosine residue in the catalytic site
RT   of a chitinase isolated from Zea mays that is selectively modified
RT   during inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-
RT   carbodiimide.";
RL   J. Biol. Chem. 267:3886-3893(1992).
CC   -!- FUNCTION: Defense against chitin containing fungal pathogens.
CC   -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-
CC       glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
CC   -!- MISCELLANEOUS: Maize chitinase B seems to be less active than
CC       chitinase A.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily.
CC   -!- SIMILARITY: Contains 1 chitin-binding type-1 domain.
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DR   EMBL; M84165; AAA33445.1; -; Genomic_DNA.
DR   PIR; B42424; B42424.
DR   HSSP; P02877; 1HEV.
DR   Gramene; P29023; -.
DR   MaizeGDB; 25130; -.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004568; F:chitinase activity; IEA:InterPro.
DR   GO; GO:0016998; P:cell wall catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR   InterPro; IPR001002; Chitin_bd_1.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   PANTHER; PTHR22595; Glyco_hydro_19_cat; 1.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   ProDom; PD000609; Chitin_binding_1; 1.
DR   ProDom; PD354900; Glyco_hydro_19; 1.
DR   SMART; SM00270; ChtBD1; 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   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Plant defense;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL       <1     20       Potential.
FT   CHAIN        21    269       Endochitinase B.
FT                                /FTId=PRO_0000005304.
FT   DOMAIN       21     55       Chitin-binding type-1.
FT   REGION       58     66       Hinge region (Gly-rich).
FT   REGION       67    269       Catalytic.
FT   DISULFID     23     31       By similarity.
FT   DISULFID     25     37       By similarity.
FT   DISULFID     30     44       By similarity.
FT   DISULFID     48     53       By similarity.
FT   DISULFID     89    138       By similarity.
FT   DISULFID    150    159       By similarity.
FT   DISULFID    237    269       By similarity.
FT   NON_TER       1      1
SQ   SEQUENCE   269 AA;  28166 MW;  3D38B1BADF75DE8F CRC64;
     PQLVALGLAL LCAVAGPAAA QNCGCQPNVC CSKFGYCGTT DEYCGDGCQS GPCRSGRGGG
     GSGGGGANVA SVVTSSFFNG IKNQAGSGCE GKNFYTRSAF LSAVKGYPGF AHGGSQVQGK
     REIAAFFAHA THETGHFCYI SEINKSNAYC DPTKRQWPCA AGQKYYGRGP LQISWNYNYG
     PAGRAIGFDG LGDPGRVARD AVVAFKAALW FWMNSVHGVV PQGFGATTRA MQRALECGGN
     NPAQMNARVG YYRQYCRQLG VDPGPNLTC
//