ID   CELB_ASPOR              Reviewed;         416 AA.
AC   Q2TX26; O13455;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-MAY-2023, entry version 86.
DE   RecName: Full=Endo-beta-1,4-glucanase celB;
DE            Short=Endoglucanase celB;
DE            EC=3.2.1.4;
DE   AltName: Full=Carboxymethylcellulase celB;
DE   AltName: Full=Cellulase B;
DE   Flags: Precursor;
GN   Name=celB; ORFNames=AO090010000314;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=KBN616;
RX   PubMed=9008887; DOI=10.1007/s002530050857;
RA   Kitamoto N., Go M., Shibayama T., Kimura T., Kito Y., Ohmiya K.,
RA   Tsukagoshi N.;
RT   "Molecular cloning, purification and characterization of two endo-1,4-beta-
RT   glucanases from Aspergillus oryzae KBN616.";
RL   Appl. Microbiol. Biotechnol. 46:538-544(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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:9008887}.
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 4.0. Stable between pH 3.0 and 7.0.
CC         {ECO:0000269|PubMed:9008887};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius. Stable up to 50 degrees
CC         Celsius. {ECO:0000269|PubMed:9008887};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D83732; BAA22589.1; -; Genomic_DNA.
DR   EMBL; AP007175; BAE66197.1; -; Genomic_DNA.
DR   RefSeq; XP_001827330.1; XM_001827278.1.
DR   AlphaFoldDB; Q2TX26; -.
DR   SMR; Q2TX26; -.
DR   STRING; 510516.Q2TX26; -.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   GlyCosmos; Q2TX26; 8 sites, No reported glycans.
DR   EnsemblFungi; BAE66197; BAE66197; AO090010000314.
DR   GeneID; 5999464; -.
DR   KEGG; aor:AO090010000314; -.
DR   VEuPathDB; FungiDB:AO090010000314; -.
DR   HOGENOM; CLU_020817_0_1_1; -.
DR   OMA; GCVAQDT; -.
DR   OrthoDB; 3014058at2759; -.
DR   Proteomes; UP000006564; Chromosome 8.
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   GO; GO:0009251; P:glucan catabolic process; IDA:AspGD.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   PANTHER; PTHR33753:SF1; ENDO-BETA-1,4-GLUCANASE CELB; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..416
FT                   /note="Endo-beta-1,4-glucanase celB"
FT                   /id="PRO_0000395157"
FT   ACT_SITE        214
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        48
FT                   /note="V -> L (in Ref. 1; BAA22589)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   416 AA;  44448 MW;  437ADE03BF84AB53 CRC64;
     MIWTLAPFVA LLPLVTAQQV GTTADAHPRL TTYKCTSQNG CTRQNTSVVL DAATHFIHKK
     GTQTSCTNSN GLDTAICPDK QTCADNCVVD GITDYASYGV QTKNDTLTLQ QYLQTGNATK
     SLSPRVYLLA EDGENYSMLK LLNQEFTFDV DASTLVCGMN GALYLSEMEA SGGKSSLNQA
     GAKYGTGYCD AQCYTTPWIN GEGNTESVGS CCQEMDIWEA NARATGLTPH PCNTTGLYEC
     SGSGCGDSGV CDKAGCGFNP YGLGAKDYYG YGLKVNTNET FTVVTQFLTN DNTTSGQLSE
     IRRLYIQNGQ VIQNAAVTSG GKTVDSITKD FCSGEGSAFN RLGGLEEMGH ALGRGMVLAL
     SIWNDAGSFM QWLDGGSAGP CNATEGNPAL IEKLYPDTHV KFSKIRWGDI GSTYRH
//