CHIB_POPTR
ID CHIB_POPTR Reviewed; 303 AA.
AC P29031;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Acidic endochitinase WIN6.2B;
DE EC=3.2.1.14;
DE Flags: Precursor;
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1912489; DOI=10.1007/bf00037049;
RA Davis J.M., Clarke H.R.G., Bradshaw H.D. Jr., Gordon M.P.;
RT "Populus chitinase genes: structure, organization, and similarity of
RT translated sequences to herbaceous plant chitinases.";
RL Plant Mol. Biol. 17:631-639(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually;
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S.,
RA Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J.,
RA Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y.,
RA Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.S.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
CC -!- FUNCTION: Defense against chitin-containing fungal pathogens.
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 -!- INDUCTION: By wounding.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I 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; X59995; CAA42612.1; -; Genomic_DNA.
DR EMBL; CM009298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P29031; -.
DR SMR; P29031; -.
DR STRING; 3694.POPTR_0790s00220.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR Proteomes; UP000006729; Chromosome 9.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.10; -; 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 Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF57016; SSF57016; 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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..303
FT /note="Acidic endochitinase WIN6.2B"
FT /id="PRO_0000005317"
FT DOMAIN 22..62
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 82..303
FT /note="Chitinase"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 24..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 33..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 38..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 56..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 253..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 303 AA; 32209 MW; 0E0D011DFA5CC8B8 CRC64;
MSVWAFAFFS LFLSLSVRGS AEQCGQQAGD ALCPGGLCCS SYGWCGTTAD YCGDGCQSQC
DGGGGGGGGG GGGGGGGGGG GDGYLSDIIP ESMFDDMLKY RNDPQCPAVG FYTYNAFISA
AKEFPDFGNT GDDLMRKREI AAFLGQTSHE TNGWWPAAQG DQYDWGYCHM NYNYGLCGDD
LNLPLLQEPE LVETDPFIAF KTALWFWMTP QSPKPSCHAV ITESWTPSAA DSEAGRVPGY
GVITNIINGG IECGQGGPNN ANENRIGFYK TYCDSLGTTY GSNLDCYQQR PFGYGLLGLK
DTM
