ID A0A0C5FYW7_9ACTN Unreviewed; 747 AA.
AC A0A0C5FYW7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=TU94_31425 {ECO:0000313|EMBL:AJP05267.1};
OS Streptomyces cyaneogriseus subsp. noncyanogenus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP05267.1, ECO:0000313|Proteomes:UP000032234};
RN [1] {ECO:0000313|EMBL:AJP05267.1, ECO:0000313|Proteomes:UP000032234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP05267.1,
RC ECO:0000313|Proteomes:UP000032234};
RA Wang H., Li C., Xiang W., Wang X.;
RT "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL Submitted (FEB-2015) 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; CP010849; AJP05267.1; -; Genomic_DNA.
DR RefSeq; WP_044386834.1; NZ_CP010849.1.
DR AlphaFoldDB; A0A0C5FYW7; -.
DR STRING; 477245.TU94_31425; -.
DR KEGG; scw:TU94_31425; -.
DR PATRIC; fig|477245.3.peg.6694; -.
DR HOGENOM; CLU_006010_0_0_11; -.
DR OrthoDB; 9808897at2; -.
DR Proteomes; UP000032234; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000032234};
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_5005111554"
FT DOMAIN 33..154
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 182..264
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 275..739
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; 80257 MW; 33DD2247E6F45A3E CRC64;
MKRRRTALLS LTALLAGALT ALPAAQAGAE EVEQVRNGTF DSGTAPWWTS ANVTAGVTEG
RLCADVPGGT TNRWDAAVGQ NDIPLVKGES YRFSFYADGT PADHVVRAVV GLSVDPYDAY
YEVSPQLSVS GNRYSYTFTS PVDTAQGQVA FQVGGSADPW RFCLDDVSLL GGVTPEPYEP
DTGPRVRVNQ VAYLPAGPKN ATLVTDATSP LPWKLKNGDG AVAARGWTVS RGTDASSGQN
VHSIDFGGFR TRGKGFTLVA DGESSRPFDI GTDAYERLSL DAAKFYYTQR SGLAIRDDLR
PGYARPAGHV GVAPNQGDTD VPCQPGVCDY RLDVSGGWYD AGDHGKYVVN GGISVWELLS
TYERALHART GQPEKFRDGS LAIPESGNKV PDLLDEVRWE LDFLLKMQVP DGQPLAGMAH
HKIHDENWTG LPLLPSDDPQ KRELHPPTTA ATLNLAAAAA QAARLYKPYD PGFAATALAA
ARKAWAAAQA HPDVYASESD GIGGGAYPDR NIDDEFYWAA AELYLTTGEK RFADHVLNSP
VHTADIFGPT GFDWARTAAA ARLDLATVPS RLPGRDKVRQ SVVKGADRYL ATLKAHPYGM
PYAPDGNLYD WGSSHQVLNN AVVLAAAYDI TGGTKYRDGA VQSMDYILGR NALNISYVTG
YGDVTAQNQH SRWYARQLDP NLPNPPAGSL SGGPNSSIQD PVAQSKLQGC VGQFCYLDDI
QSWSTNEITI NWNAALTWMA SFVADQG
//
