CHIT5_LOTJA
ID CHIT5_LOTJA Reviewed; 397 AA.
AC A0A1B1J8Z2;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Class V chitinase CHIT5 {ECO:0000303|PubMed:27383628};
DE Short=LjCHIT5 {ECO:0000303|PubMed:27383628};
DE EC=3.2.1.14 {ECO:0000269|PubMed:27383628};
DE Flags: Precursor;
GN Name=CHIT5 {ECO:0000303|PubMed:27383628};
OS Lotus japonicus (Lotus corniculatus var. japonicus).
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; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-397, FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION BY FUSARIUM OXYSPORUM.
RC STRAIN=cv. Miyakojima MG-20; TISSUE=Root;
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 FUNCTION, MUTAGENESIS OF GLU-166 AND PRO-168, AND DISRUPTION PHENOTYPE.
RX PubMed=30284535; DOI=10.7554/elife.38874;
RA Malolepszy A., Kelly S., Soerensen K.K., James E.K., Kalisch C.,
RA Bozsoki Z., Panting M., Andersen S.U., Sato S., Tao K., Jensen D.B.,
RA Vinther M., Jong N., Madsen L.H., Umehara Y., Gysel K., Berentsen M.U.,
RA Blaise M., Jensen K.J., Thygesen M.B., Sandal N., Andersen K.R.,
RA Radutoiu S.;
RT "A plant chitinase controls cortical infection thread progression and
RT nitrogen-fixing symbiosis.";
RL Elife 7:0-0(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 inhibit hyphal growth
CC of the fungus Trichoderma viride in an agar-plate bioassay
CC (PubMed:27383628). Involved in symbiotic signaling (PubMed:30284535).
CC Required for root hair infection threads (ITs) elongation and nodule
CC development (PubMed:30284535). Possesses Nod factor (NF) hydrolase
CC activity (PubMed:30284535). NFs are lipo-chitooligosaccharide signaling
CC molecules produced by nitrogen-fixing rhizobia to initiate nodulation
CC (symbiosis) on the roots of legumes (PubMed:30284535). Modulates NF
CC levels and signaling to complete transition of infected nodules to
CC functional nitrogen-fixing organs (PubMed:30284535).
CC {ECO:0000269|PubMed:27383628, ECO:0000269|PubMed:30284535}.
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 -!- INDUCTION: Induced by the fungal pathogen Fusarium oxysporum.
CC {ECO:0000269|PubMed:27383628}.
CC -!- DISRUPTION PHENOTYPE: Root nodule development arrested at the primordia
CC stage and defect in nitrogen-fixing symbiosis in presence of
CC Mesorhizobium loti. {ECO:0000269|PubMed:30284535}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; KU041645; ANS10044.1; -; mRNA.
DR AlphaFoldDB; A0A1B1J8Z2; -.
DR SMR; A0A1B1J8Z2; -.
DR UniPathway; UPA00349; -.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
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:0009877; P:nodulation; IMP: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; Nodulation; Plant defense; Polysaccharide degradation; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..397
FT /note="Class V chitinase CHIT5"
FT /id="PRO_0000445936"
FT DOMAIN 54..397
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 166
FT /note="E->K: Root nodule development arrested at the
FT primordia stage and defect in nitrogen-fixing symbiosis in
FT presence of Mesorhizobium loti."
FT /evidence="ECO:0000269|PubMed:30284535"
FT MUTAGEN 168
FT /note="P->L: In chit5-2; Root nodule development arrested
FT at the primordia stage and defect in nitrogen-fixing
FT symbiosis in presence of Mesorhizobium loti."
FT /evidence="ECO:0000269|PubMed:30284535"
SQ SEQUENCE 397 AA; 44362 MW; 72665DD8C66BABB2 CRC64;
MIIKLLVALI HYLHETMAVQ SIITTPLLVI LMSLRSYAFT EPSLHRQQPP SKGGVRAAYW
PAWSDFSTSS IDTNYFTHIY YAFVQPAPES FNLEITESYK KWAPKYDGIH NIRPRVTTLL
SIGGGGNNAT LFSEMASSKQ NRASFINSTI HVARKHEFNG LDLDWEWPGD EKDMSNLALL
LKEWYKALVV EANTSRKSRL LLTSAVYFNS TISLIGNGPR SYPVRAIRKY LDWASPMCFD
YNGAWANETG FNAALYDPNS NISTKYGIGS WIGSGVPAEK LVMGLPLYGR AWELKDPNDH
GVGAKAVGPA VDTDGSMDYD EILVFNKDTG AKVVYDEVAV SFYSYSGTTW IGYDDGPSIT
KKVQFARSMG LKGYFFWAIG KDKDWTISKQ ASNAWGY
