ID C5X1P0_SORBI Unreviewed; 620 AA.
AC C5X1P0;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=SORBI_3001G384600 {ECO:0000313|EMBL:EER92322.1};
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:EER92322.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER92322.1, 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 -!- 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; CM000760; EER92322.1; -; Genomic_DNA.
DR RefSeq; XP_002465324.1; XM_002465279.1.
DR AlphaFoldDB; C5X1P0; -.
DR STRING; 4558.C5X1P0; -.
DR EnsemblPlants; EER92322; EER92322; SORBI_3001G384600.
DR GeneID; 8084557; -.
DR Gramene; EER92322; EER92322; SORBI_3001G384600.
DR KEGG; sbi:8084557; -.
DR eggNOG; ENOG502QUUK; Eukaryota.
DR HOGENOM; CLU_008926_1_3_1; -.
DR InParanoid; C5X1P0; -.
DR OMA; GKHYPKH; -.
DR OrthoDB; 1347382at2759; -.
DR Proteomes; UP000000768; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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:SF36; ENDOGLUCANASE 25; 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 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..585
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 515
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 563
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 572
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 620 AA; 68549 MW; FAB454FAD920E574 CRC64;
MSMYGRDPWG GPLEICHPDS ATDDDRSRNL DIDRGAMSRT LDETQQSWLL AGPGDQARKK
KKYVDIGCLV VSRKLFVWTL GVLLAAAVFA GVVAGIAKAI PRRHRPPPPP DDYTVALHKA
LMFFNAQRSG KLPKHNNIPW RGNSCMKDGL SDPAVRRSLV GGYYDAGGAV KFNFPAAFSM
TLLSWSVIEY SAKYDAVGEL GHVRDIIKWG SDYFLKTFNS TADSIDRVIA QVGSAAMSPG
STQPNDQYCW MRPEDIDYPR PVVECHACSD LAAEMAAALA AASIVFKDNK AYSQKLVHGA
TTLFQFARER RGRYSAGGSD ATKFYNSTSY WDEFVWGSSW MYLATGNSSY LTLATHPKLA
KHAGAFWGGP DYGVFSWDNK LTGAQVLLSR LRLFLSPGYP YEEMLRAFHN QTSIIMCSYL
PIFKSFNRTR GGLIQLNHGK PQPLQYVVNA AFLASVFSDY LEAADTPGWY CGPHFYSIEV
LRSFARTQIE YILGKNPLKM SYVVGFGNHY PKHVHHRGAS IPKNGVHYGC KGGWKWRDTK
KPNPNIIVGA MVAGPDRHDR FKDARKNYNY TEATLVGNAG LVAALVALSG EGHGVDKNAM
FSAVPPMFPS PPPPPAPWKP
//
