GUN5_ORYSJ
ID GUN5_ORYSJ Reviewed; 534 AA.
AC Q67UW5; A0A0N7KEP7; Q0E3W7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Endoglucanase 5;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 5;
DE Flags: Precursor;
GN OrderedLocusNames=Os02g0151300, LOC_Os02g05744; ORFNames=OSJNBa0050G13.22;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK120536; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AK120536; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AP005412; BAD38054.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07821.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77009.1; -; Genomic_DNA.
DR EMBL; AK120536; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015625427.1; XM_015769941.1.
DR AlphaFoldDB; Q67UW5; -.
DR SMR; Q67UW5; -.
DR STRING; 4530.OS02T0151300-01; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; Q67UW5; -.
DR PRIDE; Q67UW5; -.
DR EnsemblPlants; Os02t0151300-01; Os02t0151300-01; Os02g0151300.
DR GeneID; 4328316; -.
DR Gramene; Os02t0151300-01; Os02t0151300-01; Os02g0151300.
DR KEGG; osa:4328316; -.
DR eggNOG; ENOG502QRF6; Eukaryota.
DR HOGENOM; CLU_008926_1_4_1; -.
DR InParanoid; Q67UW5; -.
DR OMA; GADHNAG; -.
DR OrthoDB; 1195424at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Cellulose degradation; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..534
FT /note="Endoglucanase 5"
FT /id="PRO_0000249282"
FT REGION 515..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 484
FT /evidence="ECO:0000250"
FT ACT_SITE 493
FT /evidence="ECO:0000250"
SQ SEQUENCE 534 AA; 58556 MW; 9BA71564266869E2 CRC64;
MSDVSGRFVV AAAVVAVSLA MAAAAAAHDY GEALSKSLLY FEAQRSGRLP YNQRVRWRGH
SGLTDGLEQG VDLVGGYYDA GDHVKFGLPM AFTVTMLSWS VLEYGEEIAA AGELGHALHA
IKWGTDYFIK AHTHPNVLWT QVGDGDSDHY CWQRPEDMTT SRHAYKVDAE NPGSEVAAET
AAAMAAASIV FRRAGDAHYA HLLLHHAQQL FEFGDKYRGR YDESVEVVKN YYPSSSGYKD
ELLWAALWLH RATGRREYLD YAVDNADDFG GTGWAVSEFS WDIKYAGLQV LASKLLVEEK
HLSSQQREVL EKYRSKAEYY VCSCMGRNPG GAAHNAGRTP AGLLFIRPWN NLQYVSNAAF
LLTVYSDVLS YLSLPLLCPD PDAAADEAAP AAADAGEVLE FARSQADYIL GTNPMATSYL
VGYGEAYPRR VHHRAASSAS YARDRDFIGC LQGFDSWYSA AAENPHDLVG AVVGGPNGND
VFTDHRGAYM QTEACTYNTA PMVGVFSRLM ELERRRRGED APPSSTSPVA EDDL