ID D9Y242_9ACTN Unreviewed; 747 AA.
AC D9Y242;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=SSRG_05839 {ECO:0000313|EMBL:EFL43035.1};
OS Streptomyces griseoflavus Tu4000.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL43035.1, ECO:0000313|Proteomes:UP000002968};
RN [1] {ECO:0000313|EMBL:EFL43035.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL43035.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL Submitted (FEB-2009) 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|RuleBase:RU361166};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|PROSITE-ProRule:PRU10060, ECO:0000256|RuleBase:RU361166}.
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DR EMBL; GG657758; EFL43035.1; -; Genomic_DNA.
DR RefSeq; WP_004935617.1; NZ_GG657758.1.
DR AlphaFoldDB; D9Y242; -.
DR STRING; 467200.SSRG_05839; -.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_006010_0_0_11; -.
DR OrthoDB; 9808897at2; -.
DR Proteomes; UP000002968; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR004197; Cellulase_Ig-like.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00698; GH9_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Cellulose degradation {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 Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 30..747
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5005127481"
FT DOMAIN 33..154
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 182..265
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 275..738
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT ACT_SITE 718
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 727
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 747 AA; 80178 MW; 66103348C5AFA3EB CRC64;
MNRRRTALLS LTGLLAAALT ALPAAPAGAD PAEQVRNGTF DTGTESWWAS ANVTAAPSGG
RLCADVPGGT ANRWDAAVGQ NDITLVKGES YRFSFSAAGT PAGHTVRAIV GLQTAPYDTY
YEVSPQLGVS GDTYTYTFTS PVDTAQGQVG LQLGGSADPW RFCVDDVSLL GGVAPEPYEP
DTGPRVRVNQ VAYLPSGPKN ATLVTEAAER LPWQLKDHAG HVVGRGWTVP RGVDGSSGEN
VHSIDFGAHR GRGSGYTLTV DGETSRPFDI DASAYERLRL DSAKYYYTQR SGTEIRDDLR
PGYGRAAGHV GVAPNRGDTE VPCQPGVCDY TLDVSGGWYD AGDHGKYVVN GGISTWEVLS
TYERARHART GEPGRLGDGT LDIPESGNKV PDILDEARWE LEFLLKMQVP DGEPLAGTAH
HKIHDEQWTG LPLLPGADPQ KRELHPPTTA ATLNLAATAA QAARLYRPYD KKFAATTLAA
ARKAWTAALA HPDLLADPDD GTGGGAYPDD TVSDEFYWAA AELYLTTGER RFEEYLRDSP
VHTADIFGPL GFDWSRTAAA GRLDLATVPN RLPGGDKVRR SVVEGADRYL ATLEAHPYGM
PYAPAGNVYD WGSTHQVLNN AVVLATAYDL TGAAKYRDGA LQSMDYVLGR NALNISYVTG
YGEVNAHNQH SRWYARQLDA NLPNPPAGTL SGGPNSSIQD PYAQSKLQGC VGQFCYIDDI
QSWSTNEHTI NWNAALTRMA SFVADQG
//
