ID   Q9ZSP9_SOLLC            Unreviewed;       625 AA.
AC   Q9ZSP9;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   02-SEP-2026, entry version 146.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   Name=Cel8 {ECO:0000313|EMBL:AAD08699.1};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081 {ECO:0000313|EMBL:AAD08699.1};
RN   [1] {ECO:0000313|EMBL:AAD08699.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Hypocotyl {ECO:0000313|EMBL:AAD08699.1};
RA   Catala C., Bennett A.B.;
RT   "Cloning and sequence analysis of TomCel8; a new plant endo-beta-1,4-D-
RT   glucanase gene, encoding a protein with a putative carbohydrate binding
RT   domain (Accession No. AF098292) (PGR98-209).";
RL   Plant Physiol. 118:1535-1535(1998).
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:PRU10059,
CC       ECO:0000256|RuleBase:RU361166}.
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DR   EMBL; AF098292; AAD08699.1; -; mRNA.
DR   RefSeq; NP_001234172.1; NM_001247243.3.
DR   AlphaFoldDB; Q9ZSP9; -.
DR   SMR; Q9ZSP9; -.
DR   STRING; 4081.Q9ZSP9; -.
DR   CAZy; CBM49; Carbohydrate-Binding Module Family 49.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   PaxDb; 4081-Q9ZSP9; -.
DR   GeneID; 543583; -.
DR   Gramene; Solyc08g082250.3.1; Solyc08g082250.3.1; Solyc08g082250.3.
DR   KEGG; sly:543583; -.
DR   eggNOG; ENOG502QRF6; Eukaryota.
DR   HOGENOM; CLU_008926_1_4_1; -.
DR   OMA; WGPPEEY; -.
DR   OrthoDB; 10257085at2759; -.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   FunFam; 1.50.10.10:FF:000020; Endoglucanase; 1.
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   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 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; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   2: Evidence at transcript level;
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           22..625
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5014486871"
FT   DOMAIN          533..613
FT                   /note="Carbohydrate binding"
FT                   /evidence="ECO:0000259|SMART:SM01063"
FT   REGION          502..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..511
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        462
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        471
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   625 AA;  68923 MW;  F2999AAB2DE47C0F CRC64;
     MKGFVGSLVF VILLVVPVAL AGHNYGEALS KSFLFYEAQR SGYLPRNQRV QWRGNSGLND
     GKASGIDLVG GYYDAGDNVK FGLPMAFTVT MLSWSILEYG RQMAASGELS HAMDAVKWGT
     DYLLKAHPEP YVLYGEVGDG NTDHYCWQRP EDMTTSRAAY RIDPNHPGSD LAGETAAAMA
     AASIVFRRYN PGYSNELLNH AHQLFEFADK YRGKYDSSIT VAQKYYRSVS GYADELLWGA
     AWLYKASNNQ FYLNYLGRNG DALGGTGWSM TEFGWDVKYA GVQTLVAQFL MSGKAGHNAP
     VFEKYQQKAE NFMCSMLGKG NRNTQKTPGG LIYRQRWNNM QFVTSAAFLA TTYSDYLASA
     GKYLKCSSGF VSPNELLSFA KSQVDYILGD NPRATSYMVG YGNNYPRQVH HRASSIVSFK
     VNPSFVSCRG GYATWYSRKA SDPNLLTGAL VGGPDAYDNF ADQRDNYEQT EPATYNNAPL
     IGVLARLHAG HSGYNQLLPV VPDPKPTPKP APRTKVTPAP RPRVLPVPAN AHVTIQQRAT
     SSWALNGKTY YRYSAVVTNK SGKTVKNLKL SIVKLYGPLW GLTKYGNSFI FPAWLNSLPA
     GKSLEFVYIH TASPAIVSVS SYTLV
//