ID A0A239LSN9_9ACTN Unreviewed; 528 AA.
AC A0A239LSN9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=SAMN05421812_104568 {ECO:0000313|EMBL:SNT33546.1};
OS Asanoa hainanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Asanoa.
OX NCBI_TaxID=560556 {ECO:0000313|EMBL:SNT33546.1, ECO:0000313|Proteomes:UP000198362};
RN [1] {ECO:0000313|EMBL:SNT33546.1, ECO:0000313|Proteomes:UP000198362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5593 {ECO:0000313|EMBL:SNT33546.1,
RC ECO:0000313|Proteomes:UP000198362};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZPH01000004; SNT33546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239LSN9; -.
DR OrthoDB; 4902692at2; -.
DR Proteomes; UP000198362; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 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:UP000198362};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..528
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012512051"
FT DOMAIN 423..528
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 528 AA; 55989 MW; EA847F2F5FCFE004 CRC64;
MQRKPVRAAL VAVLVAAATV LVAVGLTSGP ALAAGTGTGY LRTSGNKIVD STGATVRLTG
INWFGMETDN RTFHGLWSSN PWRNQVDTMA NLGYNTLRIP YSNDALKAGA TATGINDFVN
PDLVGNSPLQ ILDKVIAYAG SKGMRVILDR HRPTSAQQTA LWYTAAVPES TWISDWRMLA
QRYANNPTVI GADLHNEPHA EGTNPAATGA CWGCGDTNRD WRLAAERAGN AILGVQPNWL
IFVEGVSCPS GGLSNVWDGD TSNDEDCGWW GGNLSRAGQF PVRLSVANRL VYSPHDYAIS
VYHQSWFDAP DYPANLPAIW DKYWGYLFKQ NTAPIMLGEF GTTLADPKDR VWLTNLMSYL
GSGVNGMSFT YWSWNPNSGD TGGIANDDWT TINQAKQSII SPYLIAPTGG GGPTTGPTGG
PSTPPAQGDC DATYRQTNAW QGGFQGELTV TNRGTAPVNP WRVTWTWPSG VTLGSGWNAT
VTQSGTTITA AAPTWSPALA PGASVTIGFT ANGTAAAPGA PALNGVAC
//
