ID A0A3M2LJ89_9ACTN Unreviewed; 810 AA.
AC A0A3M2LJ89;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=EBN88_18880 {ECO:0000313|EMBL:RMI37534.1};
OS Streptomyces triticirhizae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2483353 {ECO:0000313|EMBL:RMI37534.1, ECO:0000313|Proteomes:UP000278673};
RN [1] {ECO:0000313|EMBL:RMI37534.1, ECO:0000313|Proteomes:UP000278673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY642 {ECO:0000313|EMBL:RMI37534.1,
RC ECO:0000313|Proteomes:UP000278673};
RA Han C.;
RT "Isolation, diversity and antifungal activity of actinobacteria from
RT wheat.";
RL Submitted (OCT-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMI37534.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RFFJ01000111; RMI37534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2LJ89; -.
DR Proteomes; UP000278673; 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 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.
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}.
FT DOMAIN 88..209
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 237..320
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 330..797
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 776
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 785
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 810 AA; 85090 MW; 77BD113D1CF5FFD3 CRC64;
MPWEFLGALP QAQRPNRTPT EQRTTTAPPH TPPSVPSKDR AVTQHPSHPP HGHRRARRGK
RLLGVALGAG LIAGAITLPN AGAADGPELI VNGDFADGTT EPWWWTADNP GEVVDGQLCA
DIPGGTSNPW DAIIGQNDLA LTAGESYELS YTATATAAAS SRTAVQQAEE PYDTELSVVD
QIGTEPTTFT HVFTVGADND AAQLVFQVGG KADPYTLCLD DISLTGGAEP PVYEPDTGSP
VRVNQVGYLT EGPKQGTFVT ESTDAQTWTL NDASGAEVAT GETTPLGVDP SSEQNVQGFD
FSEVTAPGDG YTVTIGEETS EPFAIGDDLY STLRSDALAY FYHNRSGIEI DAELVGEEYA
RPAGHVNEAP NQGDDGVTCW KNECDYTLDA AGGWYDAGDH GKYVVNGGIS VAQLLSSYER
TLTTEGANGE PLGDGALAVP EQGNGVPDIL DEARWQLEFL LSMRVPEGEQ LAGMAHHKLH
DAAWTALPTL PHQDAQPREL HPVSTAATLN VAAAAAQGAR LFAEYDPEFA DELLAAAESS
YAAAVANPDL LADPNDGVGG GAYSDAKLTD EFYWAAAELF VTTGEDTYKE AVLGSELHGD
AEGVFPPGGF SWGETAALGG LSLATVPNAL SEAELAEVRA TVAEAADGLV ELAGGEAYGV
PLGVDGYVWG SNSQVLNNMV VLATAHDLTG ETAYRDAVLT GLDYLLGRNP LNLSYVTGYG
ERDVHNQHHR FWANQLDPSL PNPPAGSVAG GPNSALQDPV AEDLLQGCAP AMCYVDDIES
YSTNEITINW NAPLAWIASY ADDLGGGAAE
//
