CHT5A_MEDTR
ID CHT5A_MEDTR Reviewed; 384 AA.
AC A0A072VEP0; U5N1E1;
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 CHIT5a {ECO:0000305};
DE Short=MtCHIT5a {ECO:0000303|PubMed:24082029};
DE EC=3.2.1.14 {ECO:0000269|PubMed:27383628};
DE Flags: Precursor;
GN Name=CHIT5A {ECO:0000303|PubMed:24082029};
GN OrderedLocusNames=MTR_1g013150 {ECO:0000312|EMBL:KEH39868.1};
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 [MRNA].
RX PubMed=24082029; DOI=10.1104/pp.113.223966;
RA Tian Y., Liu W., Cai J., Zhang L.Y., Wong K.B., Feddermann N., Boller T.,
RA Xie Z.P., Staehelin C.;
RT "The nodulation factor hydrolase of Medicago truncatula: characterization
RT of an enzyme specifically cleaving rhizobial nodulation signals.";
RL Plant Physiol. 163:1179-1190(2013).
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).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
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 inhibit 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 -!- PATHWAY: Glycan degradation; chitin degradation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; KC833513; AGX84978.1; -; mRNA.
DR EMBL; CM001217; KEH39868.1; -; Genomic_DNA.
DR EMBL; PSQE01000001; RHN76982.1; -; Genomic_DNA.
DR RefSeq; XP_013465832.1; XM_013610378.1.
DR AlphaFoldDB; A0A072VEP0; -.
DR SMR; A0A072VEP0; -.
DR EnsemblPlants; KEH39868; KEH39868; MTR_1g013150.
DR GeneID; 25481955; -.
DR Gramene; KEH39868; KEH39868; MTR_1g013150.
DR KEGG; mtr:MTR_1g013150; -.
DR HOGENOM; CLU_002833_3_2_1; -.
DR OrthoDB; 826687at2759; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000002051; Chromosome 1.
DR Proteomes; UP000265566; Chromosome 1.
DR ExpressionAtlas; A0A072VEP0; 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..384
FT /note="Class V chitinase CHIT5a"
FT /id="PRO_5014500554"
FT DOMAIN 39..384
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 85
FT /note="I -> K (in Ref. 1; AGX84978)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="T -> A (in Ref. 1; AGX84978)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="S -> T (in Ref. 1; AGX84978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 43241 MW; BAC9236A23436BAA CRC64;
MAVQKIIITP ILVFLVTIFF NVSSSSSSNN SQYQFLNHGV RSAYWPAGDD FSPSLIDTNY
FTHILLAFIQ PEPISFKLEI TKSGIKWGQN FIKALRHRSP PVKTLLSIGG GGSNSTLFSE
IASTKQNREI FINSTIEVAR KYRFDGVDLD WEFPETQQDM FNLGLLYEEW YNALFAEAKV
RRKPRLLLTS AVYYNSTVRL IGKHGPRSYP TQAINKYLDW ASPMCFDYHG TWDNNTDFNA
ALYDSKSEIS TNFGLHSWIK SGVRPEKLVM GLALYGRAWE LKDPNVNGVG AEAVGPATDT
DGSMNYNEIL KFNKQSGANV VYDKVAISFY SYAGTTWIGY DDGPSITTKV RFAKSLGLKG
YFFWALGKDK DWSISKQASN AWGH
