CHT5B_MEDTR
ID CHT5B_MEDTR Reviewed; 379 AA.
AC A0A072UR65; A0A1B1J8W5;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Class V chitinase CHIT5b {ECO:0000305};
DE Short=MtCHIT5b {ECO:0000303|PubMed:27383628};
DE EC=3.2.1.14 {ECO:0000269|PubMed:27383628};
DE Flags: Precursor;
GN Name=CHIT5B {ECO:0000303|PubMed:27383628};
GN OrderedLocusNames=MTR_4g117000 {ECO:0000312|EMBL:KEH32177.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION BY FUSARIUM OXYSPORUM, AND MUTAGENESIS OF PRO-224;
RP ARG-225; SER-289 AND LEU-296.
RX PubMed=27383628; DOI=10.1098/rsob.160061;
RA Zhang L.Y., Cai J., Li R.J., Liu W., Wagner C., Wong K.B., Xie Z.P.,
RA Staehelin C.;
RT "A single amino acid substitution in a chitinase of the legume Medicago
RT truncatula is sufficient to gain Nod-factor hydrolase activity.";
RL Open Biol. 6:0-0(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
CC -!- FUNCTION: Possesses chitinase activity in vitro toward glycol chitin,
CC carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides
CC (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5 (PubMed:27383628).
CC Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3
CC molecules (PubMed:27383628). Has the capacity to reduce hyphal growth
CC of the fungus Trichoderma viride in an agar-plate bioassay
CC (PubMed:27383628). {ECO:0000269|PubMed:27383628}.
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:0000255|PROSITE-ProRule:PRU10053,
CC ECO:0000269|PubMed:27383628};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.5 mM for (GlcNAc)6 {ECO:0000269|PubMed:27383628};
CC KM=8.6 mM for (GlcNAc)5 {ECO:0000269|PubMed:27383628};
CC -!- PATHWAY: Glycan degradation; chitin degradation. {ECO:0000305}.
CC -!- INDUCTION: Induced by the fungal pathogen Fusarium oxysporum.
CC {ECO:0000269|PubMed:27383628}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; KU041646; ANS10045.1; -; Genomic_DNA.
DR EMBL; CM001220; KEH32177.1; -; Genomic_DNA.
DR EMBL; PSQE01000004; RHN64104.1; -; Genomic_DNA.
DR RefSeq; XP_013458146.1; XM_013602692.1.
DR AlphaFoldDB; A0A072UR65; -.
DR SMR; A0A072UR65; -.
DR EnsemblPlants; KEH32177; KEH32177; MTR_4g117000.
DR GeneID; 25493984; -.
DR Gramene; KEH32177; KEH32177; MTR_4g117000.
DR KEGG; mtr:MTR_4g117000; -.
DR HOGENOM; CLU_002833_3_2_1; -.
DR OrthoDB; 826687at2759; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000002051; Chromosome 4.
DR Proteomes; UP000265566; Chromosome 4.
DR ExpressionAtlas; A0A072UR65; differential.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
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 SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Plant defense; Polysaccharide degradation; Reference proteome;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..379
FT /note="Class V chitinase CHIT5b"
FT /id="PRO_5014499891"
FT DOMAIN 34..379
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 224
FT /note="P->S: No effect on chitinase activity. Confers Nod
FT factor hydrolase activity; when associated with G-225."
FT /evidence="ECO:0000269|PubMed:27383628"
FT MUTAGEN 225
FT /note="R->G: No effect on chitinase activity. Confers Nod
FT factor hydrolase activity; when associated with S-224."
FT /evidence="ECO:0000269|PubMed:27383628"
FT MUTAGEN 289
FT /note="S->A,K,P: No effect on chitinase activity."
FT /evidence="ECO:0000269|PubMed:27383628"
FT MUTAGEN 289
FT /note="S->P: Confers Nod factor hydrolase activity."
FT /evidence="ECO:0000269|PubMed:27383628"
FT MUTAGEN 296
FT /note="L->G: No effect on chitinase activity."
FT /evidence="ECO:0000269|PubMed:27383628"
FT CONFLICT 27
FT /note="Missing (in Ref. 1; ANS10045)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="T -> I (in Ref. 1; ANS10045)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="L -> F (in Ref. 1; ANS10045)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="C -> R (in Ref. 1; ANS10045)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="D -> N (in Ref. 1; ANS10045)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="D -> N (in Ref. 1; ANS10045)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="M -> L (in Ref. 1; ANS10045)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="N -> D (in Ref. 1; ANS10045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 41526 MW; 01AF996A5B58C572 CRC64;
MANILNLKHL LTLALILLAL ATKSSTSSSS SITRVKGIYW LENPFFPPTT VDTSLFTHIF
YSFLTPNNIT YKLEISSSQI LSLNTFTKTF KTKSPPAATL FSIGGAGSNS SLLAFIASDP
PACAAFINST IDVARTFGFD GIDLDWEFPK NTKEMNDLGE MLFQWRKAIS DEGATTGRPP
LLLTAAVYFA VNFSIYGEPR MYPVNSINEN LDWVNVMSYE LRGPRSNKTG APSGTFDPKS
NVSVVSGLLS WIHSGVVPEK LVMGMPLYGK SWKLRDPNVH GIGAPSVGSG PGVNGLMAYF
QVLDFNRQKS AKVEYDVDTA SVYSYSGSTW IGYDNPFTVS IKVGFAQALK LRGYFFWVAG
LDTLDWKIAT QASKAWKLV
