ID A0A1B6Q0Y5_SORBI Unreviewed; 544 AA.
AC A0A1B6Q0Y5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=SORBI_3003G015800 {ECO:0000313|EMBL:KXG31545.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG31545.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG31545.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10060,
CC ECO:0000256|RuleBase:RU361166}.
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DR EMBL; CM000762; KXG31545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6Q0Y5; -.
DR STRING; 4558.A0A1B6Q0Y5; -.
DR EnsemblPlants; KXG31545; KXG31545; SORBI_3003G015800.
DR Gramene; KXG31545; KXG31545; SORBI_3003G015800.
DR InParanoid; A0A1B6Q0Y5; -.
DR OMA; ATEEPFY; -.
DR Proteomes; UP000000768; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
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; IPR019028; CBM_49.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF190; ENDOGLUCANASE 2; 1.
DR Pfam; PF09478; CBM49; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM01063; CBM49; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 451..530
FT /note="Carbohydrate binding"
FT /evidence="ECO:0000259|SMART:SM01063"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 388
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 544 AA; 58019 MW; ACD960E65C78395A CRC64;
MGAPPEPHGL AASSGRKEAT QGRKLADEEG GQQRRRGGEG GERRHGSTSG AAGLAASPDL
GWEETLEGGR EGREGRREEA VQGRALTGKG ADDDDNNGGE TEFTRKLGSL LEKHGFSHSE
CVGVLLFDFA DKYRGRYDSS ITVARKYYAS SSGYGAELLW AAAWLHEATG ESRYLDYLAT
NADALGGTGW SINQFGWDVK YPGVQVLAAM FLLRRGGNAG AHANVLRRYK QKADLFACSC
LGRGGANSVR RTPGGMVYHQ SWNNVQFVTS AAFLLAAYAD HLAAAGQAAQ CPSGGSSAQP
SELLAFARSQ VDYILGSNPR ATSYMAHHRG ASIVSVKANP SFVSCQAGYS SWYHRRSANP
NLLDGATVGG PDEYDNFADE RDNYEQTEAT TYNNAPLMGV LARLAAGHGG GRFGHHSVAA
DLPAEASSST AINRTSLPSP TPAAPEHASP IEIEQNATAS WTERGKTYHR YAVTVTNRSL
IKTVHELHIG ISKLYGQVWG VNKARYGYVL PSGLPSLPAG KSASFVYVQA APPADVWVTG
YKLL
//
