ID   EGLB_EMENI              Reviewed;         328 AA.
AC   Q1HFS8; C8VF90; Q5B2L6;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   02-SEP-2026, entry version 90.
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; ORFNames=AN5214;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA   Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT   "Development and application of a suite of polysaccharide-degrading enzymes
RT   for analyzing plant cell walls.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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:16844780}.
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. {ECO:0000269|PubMed:16844780};
CC       Temperature dependence:
CC         Optimum temperature is 52 degrees Celsius.
CC         {ECO:0000269|PubMed:16844780};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBF81096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA62395.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DQ490496; ABF50872.1; -; mRNA.
DR   EMBL; AACD01000089; EAA62395.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001305; CBF81096.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_662818.1; XM_657726.1.
DR   AlphaFoldDB; Q1HFS8; -.
DR   SMR; Q1HFS8; -.
DR   STRING; 227321.Q1HFS8; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GlyCosmos; Q1HFS8; 1 site, No reported glycans.
DR   KEGG; ani:ANIA_05214; -.
DR   VEuPathDB; FungiDB:AN5214; -.
DR   eggNOG; ENOG502QXN4; Eukaryota.
DR   HOGENOM; CLU_029718_0_2_1; -.
DR   InParanoid; Q1HFS8; -.
DR   OrthoDB; 5823761at2759; -.
DR   Proteomes; UP000000560; Chromosome V.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IDA:UniProtKB.
DR   GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
DR   FunFam; 3.20.20.80:FF:000078; Endo-beta-1,4-glucanase B; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
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   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..328
FT                   /note="Endo-beta-1,4-glucanase B"
FT                   /id="PRO_0000394058"
FT   ACT_SITE        155
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   328 AA;  36080 MW;  7FBF3D7078476B4D CRC64;
     MKVNTLLVAV AAGTAMAAPQ LKKRAGFTFF GVTEAGAEFG EKSIPGVWGT DYTFPDTESI
     LTLISKGFNT FRIPFLMERL TPEMTGSFDE GYLKNLTSVV NAVTDAGAWA IVDAQNFGRF
     NGEIISSASD FQTWWKNVAA EFADNKNVIF DTNNEFHDMD QTLVLDLNQA AINGIRAAGA
     TSQYIFVEGN SYTGAWTWTD NNDNLKSLTD PQDKIVYEMH QYLDTDGSGT HETCVSETIG
     AERVESATQW LKDNGKLGVI GEFAGGNNEI CRAAVKSLLD ALKENDDVWL GALWWAAGPW
     WEDYMFSMEP TDGIAYTGML STLEAYMN
//