ID A0A101N5U3_9ACTN Unreviewed; 549 AA.
AC A0A101N5U3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=AQI94_17465 {ECO:0000313|EMBL:KUM87144.1};
OS Streptomyces pseudovenezuelae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM87144.1, ECO:0000313|Proteomes:UP000053039};
RN [1] {ECO:0000313|EMBL:KUM87144.1, ECO:0000313|Proteomes:UP000053039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM87144.1,
RC ECO:0000313|Proteomes:UP000053039};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT strain for the species Streptomyces pseudovenezuelae.";
RL Submitted (OCT-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|ARBA:ARBA00000966,
CC ECO:0000256|RuleBase:RU361153};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|RuleBase:RU361153}.
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:KUM87144.1}.
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DR EMBL; LMWM01000018; KUM87144.1; -; Genomic_DNA.
DR RefSeq; WP_031044610.1; NZ_KQ948147.1.
DR AlphaFoldDB; A0A101N5U3; -.
DR OrthoDB; 9801198at2; -.
DR Proteomes; UP000053039; 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 CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42754:SF1; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42754; ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW 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|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361153};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..549
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007101157"
FT DOMAIN 352..441
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 439..549
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 549 AA; 56848 MW; B4BCE5E0E459FF63 CRC64;
MSRTRKSPLR TFLARLAALV GLVVLGALCP GTAQAAQQPA AQAAGLHISN GRLVESNGND
FVMRGVNHAH TWYPNELGSL ADIKAQGANT VRVVLADGHR WTANTAADVT NVVAQCKANR
LICVLEVHDT TGYGEDSAAG TLDQAADYWI GLKDVLAGQE NYIIINIGNE PWGNTDPAGW
TAPTIAAIKK LRNAGFEHTI MVDAPNWGQD WQQVMRTNAQ SVYAADTTGN LVFSIHMYSV
FDTAAEITDY LNAFVSAKLP LVIGEFGGPA DQWGDPDEDT MMAAAEQLHI GYLAWSWSGN
TDPILDLVLD FDPARMTSWG QRIFNGANGI AQTAKEATVF GGGSSDTQAP TAPGTPTASA
VTATSARLTW TASTDNVGVA GYDVVRVSGG TETKVAAATT NSVTVTGLTA GTAYSFAVYA
RDAAGNRSAR SATVGVTTAN TPAGSCSVGY RVVGDWQGGF QGEIVIRNTG TAAVTGWKLG
FTFADGQSVT NMWGGTAAQS AGAVTVTPAS YTNTIAAGGS VTLGFIGSKG STNTAPAAFT
LNGAACVNG
//