ID A0A1I1R3D0_9ACTN Unreviewed; 638 AA.
AC A0A1I1R3D0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=SAMN05421773_112157 {ECO:0000313|EMBL:SFD28772.1};
OS Streptomyces aidingensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=910347 {ECO:0000313|EMBL:SFD28772.1, ECO:0000313|Proteomes:UP000199207};
RN [1] {ECO:0000313|EMBL:SFD28772.1, ECO:0000313|Proteomes:UP000199207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5739 {ECO:0000313|EMBL:SFD28772.1,
RC ECO:0000313|Proteomes:UP000199207};
RA de Groot N.N.;
RL Submitted (OCT-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:RU361153};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|RuleBase:RU361153}.
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DR EMBL; FOLM01000012; SFD28772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1R3D0; -.
DR STRING; 910347.SAMN05421773_112157; -.
DR OrthoDB; 4902692at2; -.
DR Proteomes; UP000199207; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51172; CBM3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361153};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000199207};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..638
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011503941"
FT DOMAIN 488..638
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT REGION 36..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..485
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 70074 MW; 5A752120B91A0133 CRC64;
MSSFTRRRSK SRRPLAAAGL VLGALLAAGL PGLAGSAGAE PAPEESGPVQ TAGAAGTDWL
TTDGNKITDQ AGNQVWLTGV NWFGFNTSER FFHGLWSANI EDVTRAVAER GFNIVRVPIS
TQLLNEWKNG QAAVASGINT YVNPELEGRT TLGVFDYWLT LCEKYGLKVM LDVHSAEADN
SGHVYPMWYK GEITSEIFYS TWEWVADRYK DNDTLVAFDI ENEPHGKANE TPRAKWDDST
DEDNWKHACE TAGKRILAIN PNMLILCEGI EVYPREGVSW TSTTPTDYYG MWWGGNLRGV
KDYPVDLGAG QDQLVYSPHD YGPSVWQQPW FEGDWNRTTL ERDVWDPNWL YIHKENTAPL
LIGEWGGHLD GGDNEKWMTA LRDMMTDYGV HHTFWCLNPN SGDTGGLLGY DWASWDEEKY
GFVEPALWSQ GGKFVGLDHE VKLGGSTSTT GISLNEYLGN PDPDPEPDPD PEPDPDPEPD
PDPEPEPGDA ALAVEYKNND SSATDNAIRP SLRLRNTGDT PVDLSTVTLR YWFTRDGASS
VSAWCDWAVV GCANLDLEVV HLPTAVNGAD SYLEVSFTSG SLAPGAGTGD LQLRMSKSDW
SAFDETDDYS HGTGTAYAET ATVTAHVNGG LVWGTEPS
//