UniProt: D7M426

Database: UniProt
Entry: D7M426_ARALL

LinkDB:  D7M426_ARALL 
Original site:  D7M426_ARALL

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   D7M426_ARALL            Unreviewed;       511 AA.
AC   D7M426;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=ARALYDRAFT_490341 {ECO:0000313|EMBL:EFH49106.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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         Evidence={ECO:0000256|ARBA:ARBA00000966,
CC         ECO:0000256|RuleBase:RU361166};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10059,
CC       ECO:0000256|RuleBase:RU361166}.
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DR   EMBL; GL348718; EFH49106.1; -; Genomic_DNA.
DR   RefSeq; XP_002872847.1; XM_002872801.1.
DR   AlphaFoldDB; D7M426; -.
DR   STRING; 81972.D7M426; -.
DR   EnsemblPlants; fgenesh2_kg.6__3475__AT4G02290.1; fgenesh2_kg.6__3475__AT4G02290.1; fgenesh2_kg.6__3475__AT4G02290.1.
DR   GeneID; 9308916; -.
DR   Gramene; fgenesh2_kg.6__3475__AT4G02290.1; fgenesh2_kg.6__3475__AT4G02290.1; fgenesh2_kg.6__3475__AT4G02290.1.
DR   KEGG; aly:9308916; -.
DR   eggNOG; ENOG502QPI6; Eukaryota.
DR   HOGENOM; CLU_008926_1_2_1; -.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
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; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF55; ENDOGLUCANASE 17; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW   ECO:0000256|RuleBase:RU361166};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   DOMAIN          48..501
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        479
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        488
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   511 AA;  56846 MW;  E96A71CE688DEEBB CRC64;
     MALLLFSSSF RVTIFLSFFF FLCNGFTYPT SSLFNTHHHR HHVAKHNYKD ALTKSILFFE
     GQRSGKLPSN QRMSWRKDSG LSDGSALHVD LVGGYYDAGD NIKFGFPMAF TTTMLSWSVI
     EFGGLMKSEL QNAKIAIRWA TDYLLKATSS PDTIYVQVGD ANKDHSCWER PEDMDTVRSV
     FKVDKNTPGS DVAAETAAAL AAAAIVFRKS DPSYSKVLLK RAIRVFAFAD KYRGTYSAGL
     KPDVCPFYCS YSGYQDELLW GAAWLQKATK NLKYLNYIKI NGQILGAAEY DNTFGWDNKH
     AGARILLTKA FLVQNVKTLH EYKGHADNFI CSVIPGAPFS STQYTPGGLL FKMADANMQY
     VTSTSFLLLT YAKYLTSAKT VVHCGGSVYT PGRLRSIAKR QVDYLLGDNP LRMSYMVGYG
     PKFPRRIHHR GSSLPCVASH PAKIQCHQGF AIMNSQSPNP NFLVGAVVGG PDQHDRFPDE
     RSDYEQSEPA TYINAPLVGA LAYFAHAYGQ L
//

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