ID A0A2C9W9V6_MANES Unreviewed; 622 AA.
AC A0A2C9W9V6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=MANES_02G010600 {ECO:0000313|EMBL:OAY56369.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY56369.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY56369.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY56369.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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; CM004388; OAY56369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9W9V6; -.
DR STRING; 3983.A0A2C9W9V6; -.
DR EnsemblPlants; OAY56369; OAY56369; MANES_02G010600.
DR Gramene; OAY56369; OAY56369; MANES_02G010600.
DR OrthoDB; 1347382at2759; -.
DR Proteomes; UP000091857; Chromosome lg2.
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 InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF19; ENDOGLUCANASE 19-RELATED; 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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 25..622
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5011831591"
FT DOMAIN 530..610
FT /note="Carbohydrate binding"
FT /evidence="ECO:0000259|SMART:SM01063"
FT ACT_SITE 413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 465
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 474
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 622 AA; 68369 MW; 308211A655D11729 CRC64;
MEKRCALFSM APLFLFLCLP FAFAGHDYGQ ALSKSILFFE AQRSGYLPHD QRVTWRANSG
LNDGKTSGVD LVGGYYDAGD NVKFGLPMAF TITMMSWSII EYGKQMAASG ELGHAMAAVK
WGTDYLIKAH PEPYVLYGEV GDGNSDHYCW QRPEDMTTDR RAYRIDPSNP GSDLAGETAA
AMAAASIVFR RSNPAYANEL LAHAHQLFDF ADKYRGKYDS SITVAQKYYR SISGYNDELL
WAAAWLYHAT NNQYYLSYLG NNGDSMGGTG WSMTEFGWDV KYAGVQTLVA KFLMQGKAGH
YAPVFERYQQ KAEYFMCSCL GKGARNVQKT PGGLIFRQRW NNLQFVSSAS FLATVYSDYL
ASSGRSMKCA SGNVAPSELL SFAKSQVDYI LGDNPRATSY MVGYGNNYPR QVHHRASSIV
SIKVDPTFVS CRGGYATWYS KKASDPNVLT GAIVGGPDAY DNFADERDNY EQTEPATYNN
APIVGILARL NGGHGGYNQL LPVVIPAPNQ QKPAPQPKIT PAPASTSVPV SIEQKVTTSW
IAKGKTYYRY STIVSNKSAK TLTDLKLTIS KLYGPIWGLN KSGDSYAFPS WLNTLPAGKS
LEFVYIHSAS AADISVSSYT LA
//
