EGLB_ASPNG
ID EGLB_ASPNG Reviewed; 331 AA.
AC O74706; Q9C3Z7;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Endo-beta-1,4-glucanase B;
DE Short=Endoglucanase B;
DE EC=3.2.1.4;
DE AltName: Full=Carboxymethylcellulase B;
DE AltName: Full=Cellulase B;
DE Flags: Precursor;
GN Name=eglB; Synonyms=eng1;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=9758775; DOI=10.1128/aem.64.10.3615-3619.1998;
RA van Peij N.N., Gielkens M.M., de Vries R.P., Visser J., de Graaff L.H.;
RT "The transcriptional activator XlnR regulates both xylanolytic and
RT endoglucanase gene expression in Aspergillus niger.";
RL Appl. Environ. Microbiol. 64:3615-3619(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=IFO 31125;
RX PubMed=16233124; DOI=10.1263/jbb.92.434;
RA Hong J., Tamaki H., Akiba S., Yamamoto K., Kumagai H.;
RT "Cloning of a gene encoding a highly stable endo-beta-1,4-glucanase from
RT Aspergillus niger and its expression in yeast.";
RL J. Biosci. Bioeng. 92:434-441(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCRC 31494;
RA Hsing-Ren W., Trong-Rong Y.;
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC glycosidic bonds, like in carboxymethylcellulose (CMC),
CC hydroxyethylcellulose (HEC) and beta-glucan. Involved in the
CC degradation of complex natural cellulosic substrates.
CC {ECO:0000269|PubMed:16233124}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:16233124};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:16233124};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Expression is under the control of the xylanolytic
CC transcriptional activator xlnR. {ECO:0000269|PubMed:9758775}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; GQ292753; ACT68011.1; -; Genomic_DNA.
DR EMBL; AF331518; AAG50051.1; -; mRNA.
DR EMBL; AJ224452; CAA11965.1; -; Genomic_DNA.
DR PDB; 5I77; X-ray; 1.80 A; A=31-330.
DR PDB; 5I78; X-ray; 1.58 A; A/B=31-330.
DR PDB; 5I79; X-ray; 2.35 A; A/B=31-330.
DR PDBsum; 5I77; -.
DR PDBsum; 5I78; -.
DR PDBsum; 5I79; -.
DR AlphaFoldDB; O74706; -.
DR SMR; O74706; -.
DR STRING; 5061.CADANGAP00006047; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; EGL5B_ASPNG; -.
DR VEuPathDB; FungiDB:An07g08950; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1164595; -.
DR VEuPathDB; FungiDB:ATCC64974_49560; -.
DR VEuPathDB; FungiDB:M747DRAFT_268418; -.
DR eggNOG; ENOG502QXN4; Eukaryota.
DR BRENDA; 3.2.1.4; 518.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..331
FT /note="Endo-beta-1,4-glucanase B"
FT /id="PRO_5000065052"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 13
FT /note="A -> G (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="S -> P (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="T -> A (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="G -> D (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="V -> I (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="I -> V (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="Q -> E (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="Y -> H (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="A -> AT (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="G -> E (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 248..250
FT /note="ITD -> VTE (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="T -> A (in Ref. 2; AAG50051)"
FT /evidence="ECO:0000305"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:5I78"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:5I79"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:5I78"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:5I78"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:5I78"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 166..182
FT /evidence="ECO:0007829|PDB:5I78"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5I78"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:5I78"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:5I78"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:5I78"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:5I78"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:5I78"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:5I78"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:5I78"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:5I78"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5I78"
SQ SEQUENCE 331 AA; 36559 MW; F3AE4BF70007C707 CRC64;
MKFQSTLLLA AAAGSALAVP HGSGHKKRAS VFEWFGSNES GAEFGTNIPG VWGTDYIFPD
PSTISTLIGK GMNFFRVQFM MERLLPDSMT GSYDEEYLAN LTTVVKAVTD GGAHALIDPH
NYGRYNGEII SSTSDFQTFW QNLAGQYKDN DLVMFDTNNE YYDMDQDLVL NLNQAAINGI
RAAGASQYIF VEGNSWTGAW TWVDVNDNMK NLTDPEDKIV YEMHQYLDSD GSGTSETCVS
GTIGKERITD ATQWLKDNKK VGFIGEYAGG SNDVCRSAVS GMLEYMANNT DVWKGASWWA
AGPWWGDYIF SLEPPDGTAY TGMLDILETY L
