CELB_ASPOR
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 25-MAY-2022, entry version 83.
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}.
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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 EnsemblFungi; BAE66197; BAE66197; AO090010000314.
DR GeneID; 5999464; -.
DR KEGG; aor:AO090010000314; -.
DR VEuPathDB; FungiDB:AO090010000314; -.
DR HOGENOM; CLU_020817_0_1_1; -.
DR OMA; VCCNEMD; -.
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; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001722; Glyco_hydro_7.
DR InterPro; IPR037019; Glyco_hydro_7_sf.
DR PANTHER; PTHR33753; PTHR33753; 1.
DR Pfam; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SUPFAM; SSF49899; SSF49899; 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
