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   27-MAR-2024, entry version 101.
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   RefSeq; XP_001391969.1; XM_001391932.2.
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   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; EGL5B_ASPNG; -.
DR   GlyCosmos; O74706; 4 sites, No reported glycans.
DR   PaxDb; 5061-CADANGAP00006047; -.
DR   EnsemblFungi; CAK45103; CAK45103; An07g08950.
DR   GeneID; 4982163; -.
DR   VEuPathDB; FungiDB:An07g08950; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1164595; -.
DR   VEuPathDB; FungiDB:ATCC64974_49560; -.
DR   VEuPathDB; FungiDB:M747DRAFT_268418; -.
DR   eggNOG; ENOG502QXN4; Eukaryota.
DR   OrthoDB; 1638835at2759; -.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   PANTHER; PTHR34142:SF6; ENDO-BETA-1,4-GLUCANASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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
//