NFH1_MEDTR
ID NFH1_MEDTR Reviewed; 385 AA.
AC U5N4E3; A0A072US44; Q84N00; Q9M6Q0;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Nod factor hydrolase protein 1 {ECO:0000303|PubMed:24082029};
DE Short=MtNFH1 {ECO:0000303|PubMed:24082029};
DE AltName: Full=Class V chitinase NFH1 {ECO:0000305};
DE AltName: Full=Mtchit5 {ECO:0000303|PubMed:15107993};
DE Flags: Precursor;
GN Name=NFH1 {ECO:0000303|PubMed:24082029};
GN Synonyms=CHIT5 {ECO:0000312|EMBL:CAD56465.1};
GN OrderedLocusNames=MTR_4g116990 {ECO:0000312|EMBL:KEH32176.1};
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].
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-335.
RX PubMed=10875337; DOI=10.1094/mpmi.2000.13.7.763;
RA Salzer P., Bonanomi A., Beyer K., Vogeli-Lange R., Aeschbacher R.A.,
RA Lange J., Wiemken A., Kim D., Cook D.R., Boller T.;
RT "Differential expression of eight chitinase genes in Medicago truncatula
RT roots during mycorrhiza formation, nodulation, and pathogen infection.";
RL Mol. Plant Microbe Interact. 13:763-777(2000).
RN [6]
RP INDUCTION.
RX PubMed=15107993; DOI=10.1007/s00425-004-1268-8;
RA Salzer P., Feddermann N., Wiemken A., Boller T., Staehelin C.;
RT "Sinorhizobium meliloti-induced chitinase gene expression in Medicago
RT truncatula ecotype R108-1: a comparison between symbiosis-specific class V
RT and defence-related class IV chitinases.";
RL Planta 219:626-638(2004).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF 229-GLY--SER-232; PRO-295 AND
RP 295-PRO--GLY-302.
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 [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=29367305; DOI=10.1105/tpc.17.00420;
RA Cai J., Zhang L.Y., Liu W., Tian Y., Xiong J.S., Wang Y.H., Li R.J.,
RA Li H.M., Wen J., Mysore K.S., Boller T., Xie Z.P., Staehelin C.;
RT "Role of the Nod factor hydrolase MtNFH1 in regulating nod factor levels
RT during rhizobial infection and in mature nodules of Medicago truncatula.";
RL Plant Cell 30:397-414(2018).
CC -!- FUNCTION: Symbiotic enzyme that hydrolytically inactivates Nod factors
CC (NFs) with a C16:2 acyl chain produced by the microsymbiont
CC Sinorhizobium meliloti (PubMed:27383628, PubMed:29367305). NFs are
CC lipo-chitooligosaccharide signaling molecules produced by nitrogen-
CC fixing rhizobia to initiate nodulation (symbiosis) on the roots of
CC legumes (PubMed:27383628, PubMed:29367305). Controls NF hydrolysis at
CC the stage of root hair infection (PubMed:29367305). Involved in the
CC regulation of growth and branching of mature nodules (PubMed:29367305).
CC Modulates NF levels and signaling to complete transition of infected
CC nodules to functional nitrogen-fixing organs (PubMed:29367305). Lacks
CC chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin,
CC colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine)
CC (GlcNAc)6 and (GlcNAc)5 (PubMed:27383628).
CC {ECO:0000269|PubMed:27383628, ECO:0000269|PubMed:29367305}.
CC -!- INDUCTION: Induced in roots by Nod factors and infection of the
CC microsymbiont Sinorhizobium meliloti. {ECO:0000269|PubMed:15107993,
CC ECO:0000269|PubMed:29367305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; AJ515476; CAD56465.1; -; Genomic_DNA.
DR EMBL; KC833515; AGX84980.1; -; Genomic_DNA.
DR EMBL; CM001220; KEH32176.1; -; Genomic_DNA.
DR EMBL; PSQE01000004; RHN64103.1; -; Genomic_DNA.
DR EMBL; AF167329; AAF67831.1; -; Genomic_DNA.
DR RefSeq; XP_013458145.1; XM_013602691.1.
DR AlphaFoldDB; U5N4E3; -.
DR SMR; U5N4E3; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EnsemblPlants; KEH32176; KEH32176; MTR_4g116990.
DR GeneID; 25493983; -.
DR Gramene; KEH32176; KEH32176; MTR_4g116990.
DR KEGG; mtr:MTR_4g116990; -.
DR HOGENOM; CLU_002833_3_2_1; -.
DR OrthoDB; 826687at2759; -.
DR Proteomes; UP000002051; Chromosome 4.
DR Proteomes; UP000265566; Chromosome 4.
DR ExpressionAtlas; U5N4E3; 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; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
DR GO; GO:0009877; P:nodulation; IMP:UniProtKB.
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 Glycoprotein; Glycosidase; Hydrolase; Nodulation; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..385
FT /note="Nod factor hydrolase protein 1"
FT /id="PRO_5004662805"
FT DOMAIN 36..385
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 233
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 MUTAGEN 229..232
FT /note="Missing: Abolishes Nod factor hydrolase activity."
FT /evidence="ECO:0000269|PubMed:27383628"
FT MUTAGEN 295..302
FT /note="Missing: Abolishes Nod factor hydrolase activity."
FT /evidence="ECO:0000269|PubMed:27383628"
FT MUTAGEN 295
FT /note="P->S: Abolishes Nod factor hydrolase activity."
FT /evidence="ECO:0000269|PubMed:27383628"
FT CONFLICT 26..29
FT /note="KSTP -> TSTT (in Ref. 1; AGX84980/CAD56465)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..44
FT /note="IE -> DR (in Ref. 1; CAD56465)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="S -> A (in Ref. 1; AGX84980/CAD56465)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Missing (in Ref. 1; AGX84980/CAD56465)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="I -> T (in Ref. 1; CAD56465)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="T -> A (in Ref. 1; AGX84980/CAD56465)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="L -> R (in Ref. 1; AGX84980)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="S -> G (in Ref. 1; CAD56465)"
FT /evidence="ECO:0000305"
FT CONFLICT 377..384
FT /note="ASKAWRPE -> GKINTLS (in Ref. 1; AGX84980)"
FT CONFLICT 377..384
FT /note="ASKAWRPE -> QGKINTL (in Ref. 1; CAD56465)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 42193 MW; 1AD7DF8334E1BD81 CRC64;
MANFLKLKQF LTLVLILLAL AAKSSKSTPS PSSTTRVKGI YWIENPLFPP SSIDTSLFTH
IFYAFVSPNK FTYKLEEEEE DSTTVATSLT TFTNTFKTKT PPIPTLLSIG GATSNSTLFA
FIASDPTARA TFINSTIQVA RTFGFDGIDF DWEFPTTTKE MNDLGELLFQ WRRAISDETA
STSRPPLLLT AAVYFAVNFF LSGERRMYPV DSINKNLDWV NVMSYDLRGS GSNVTGAPSG
MFDSKSNVSV VSGLFSWIRG GVAPEKIVMG MPLYGKSWKL QDPNVHGIGA PNVGPGPGVD
GGMAYFQVVD FNKQMGAKVV YDKETGSVYS YSGSTWIGYD DPFTVSVKVG FAQALKLGGY
FFWAAGYDTS DWKVSTASKA WRPES
