CHIC_ARATH
ID CHIC_ARATH Reviewed; 379 AA.
AC O81862; Q0WT03;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Class V chitinase {ECO:0000303|PubMed:22936594};
DE Short=AtChiC {ECO:0000303|PubMed:22936594};
DE EC=3.2.1.14 {ECO:0000269|PubMed:21390509, ECO:0000269|PubMed:22936594};
DE EC=3.2.1.200 {ECO:0000269|PubMed:21390509};
DE Flags: Precursor;
GN Name=ChiC {ECO:0000303|PubMed:22936594};
GN OrderedLocusNames=At4g19810 {ECO:0000312|Araport:AT4G19810};
GN ORFNames=T16H5.170 {ECO:0000312|EMBL:CAA19698.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, MUTAGENESIS OF GLY-99 AND GLU-140, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=22936594; DOI=10.1093/glycob/cws125;
RA Umemoto N., Ohnuma T., Mizuhara M., Sato H., Skriver K., Fukamizo T.;
RT "Introduction of a tryptophan side chain into subsite +1 enhances
RT transglycosylation activity of a GH-18 chitinase from Arabidopsis thaliana,
RT AtChiC.";
RL Glycobiology 23:81-90(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 25-379, FUNCTION, TISSUE
RP SPECIFICITY, INDUCTION BY JASMONIC ACID; ABSCISIC ACID AND SALT, CATALYTIC
RP ACTIVITY, AND ACTIVE SITE.
RC STRAIN=cv. Columbia;
RX PubMed=21390509; DOI=10.1007/s00425-011-1390-3;
RA Ohnuma T., Numata T., Osawa T., Mizuhara M., Lampela O., Juffer A.H.,
RA Skriver K., Fukamizo T.;
RT "A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic
RT properties, and crystallographic analysis.";
RL Planta 234:123-137(2011).
CC -!- FUNCTION: Can hydrolyze glycol chitin and chitin oligosaccharides (e.g.
CC N-acetylglucosamine) (GlcNAc)4, (GlcNAc)5 and (GlcNAc)6
CC (PubMed:21390509, PubMed:22936594). Hydrolyzes N-acetylglucosamine
CC oligomers producing dimers from the non-reducing end of the substrates
CC (PubMed:21390509). {ECO:0000269|PubMed:21390509,
CC ECO:0000269|PubMed:22936594}.
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:0000269|PubMed:21390509, ECO:0000269|PubMed:22936594};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of N,N'-diacetylchitobiose from the non-reducing
CC end of chitin and chitodextrins.; EC=3.2.1.200;
CC Evidence={ECO:0000269|PubMed:21390509};
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC {ECO:0000269|PubMed:21390509, ECO:0000269|PubMed:22936594}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O81862-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O81862-2; Sequence=VSP_059331;
CC -!- INDUCTION: Induced by jasmonic acid (JA), abscisic acid (ABA) and salt
CC (NaCl). {ECO:0000269|PubMed:21390509}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; AL024486; CAA19698.1; -; Genomic_DNA.
DR EMBL; AL161551; CAB78983.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84228.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66365.1; -; Genomic_DNA.
DR EMBL; BT029539; ABL66795.1; -; mRNA.
DR EMBL; AK227762; BAE99745.1; -; mRNA.
DR PIR; T04762; T04762.
DR RefSeq; NP_001319999.1; NM_001341373.1. [O81862-1]
DR RefSeq; NP_193716.1; NM_118101.4. [O81862-1]
DR PDB; 3AQU; X-ray; 2.01 A; A/B/C/D=25-379.
DR PDBsum; 3AQU; -.
DR AlphaFoldDB; O81862; -.
DR SMR; O81862; -.
DR IntAct; O81862; 1.
DR STRING; 3702.AT4G19810.1; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PaxDb; O81862; -.
DR PRIDE; O81862; -.
DR ProteomicsDB; 240891; -. [O81862-1]
DR EnsemblPlants; AT4G19810.1; AT4G19810.1; AT4G19810. [O81862-1]
DR EnsemblPlants; AT4G19810.2; AT4G19810.2; AT4G19810. [O81862-1]
DR GeneID; 827725; -.
DR Gramene; AT4G19810.1; AT4G19810.1; AT4G19810. [O81862-1]
DR Gramene; AT4G19810.2; AT4G19810.2; AT4G19810. [O81862-1]
DR KEGG; ath:AT4G19810; -.
DR Araport; AT4G19810; -.
DR TAIR; locus:2134025; AT4G19810.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_3_2_1; -.
DR InParanoid; O81862; -.
DR OMA; NPMTYDF; -.
DR OrthoDB; 826687at2759; -.
DR PhylomeDB; O81862; -.
DR BioCyc; ARA:AT4G19810-MON; -.
DR BioCyc; MetaCyc:AT4G19810-MON; -.
DR BRENDA; 3.2.1.14; 399.
DR BRENDA; 3.2.1.200; 399.
DR UniPathway; UPA00349; -.
DR PRO; PR:O81862; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81862; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR GO; GO:0008843; F:endochitinase activity; IDA:TAIR.
DR GO; GO:0035885; F:exochitinase activity; IDA:TAIR.
DR GO; GO:0006032; P:chitin catabolic process; IDA:TAIR.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
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; 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; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carbohydrate metabolism;
KW Chitin degradation; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..379
FT /note="Class V chitinase"
FT /id="PRO_5011420228"
FT DOMAIN 27..369
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258,
FT ECO:0000305|PubMed:21390509"
FT BINDING 99
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000305|PubMed:21390509"
FT BINDING 259
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000305|PubMed:21390509"
FT BINDING 348
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258,
FT ECO:0000305|PubMed:21390509"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 17..58
FT /note="Missing (in isoform 2)"
FT /id="VSP_059331"
FT MUTAGEN 99
FT /note="G->W: Reduced activity toward glycol chitin, but
FT enhanced transglycosylation reaction toward chitin
FT oligosaccharides (GlcNAc)4, (GlcNAc)5 and (GlcNAc)6."
FT /evidence="ECO:0000269|PubMed:22936594"
FT MUTAGEN 140
FT /note="E->Q: Loss of activity and increased association
FT constant for (GlcNAc)5."
FT /evidence="ECO:0000269|PubMed:22936594"
FT CONFLICT 307
FT /note="N -> S (in Ref. 4; BAE99745)"
FT /evidence="ECO:0000305"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:3AQU"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3AQU"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:3AQU"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 145..169
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 175..186
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3AQU"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 252..266
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:3AQU"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:3AQU"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:3AQU"
FT HELIX 357..368
FT /evidence="ECO:0007829|PDB:3AQU"
SQ SEQUENCE 379 AA; 41128 MW; 14BCC21DAAE330F0 CRC64;
MSSTKLISLI VSITFFLTLQ CSMAQTVVKA SYWFPASEFP VTDIDSSLFT HLFCAFADLN
SQTNQVTVSS ANQPKFSTFT QTVQRRNPSV KTLLSIGGGI ADKTAYASMA SNPTSRKSFI
DSSIRVARSY GFHGLDLDWE YPSSATEMTN FGTLLREWRS AVVAEASSSG KPRLLLAAAV
FYSNNYYSVL YPVSAVASSL DWVNLMAYDF YGPGWSRVTG PPAALFDPSN AGPSGDAGTR
SWIQAGLPAK KAVLGFPYYG YAWRLTNANS HSYYAPTTGA AISPDGSIGY GQIRKFIVDN
GATTVYNSTV VGDYCYAGTN WIGYDDNQSI VTKVRYAKQR GLLGYFSWHV GADDNSGLSR
AASQAWDATT ATTRTIQKV
