EGLA_EMENI
ID EGLA_EMENI Reviewed; 326 AA.
AC Q5BDU5; C8VSF3; Q1HFV2; Q9Y8H6;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Endo-beta-1,4-glucanase A;
DE Short=Endoglucanase A;
DE EC=3.2.1.4;
DE AltName: Full=Carboxymethylcellulase A;
DE AltName: Full=Cellulase A;
DE Flags: Precursor;
GN Name=eglA; ORFNames=AN1285;
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;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX PubMed=10386374; DOI=10.1111/j.1574-6968.1999.tb13626.x;
RA Chikamatsu G., Shirai K., Kato M., Kobayashi T., Tsukagoshi N.;
RT "Structure and expression properties of the endo-beta-1,4-glucanase A gene
RT from the filamentous fungus Aspergillus nidulans.";
RL FEMS Microbiol. Lett. 175:239-245(1999).
RN [2]
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 [3]
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 [4]
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:10386374, 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 57 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Highly expressed in presence of carboxymethylcellulose
CC (CMC). {ECO:0000269|PubMed:10386374}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; AB009402; BAA82592.1; -; Genomic_DNA.
DR EMBL; DQ490472; ABF50848.1; -; mRNA.
DR EMBL; AACD01000017; EAA65878.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF87793.1; -; Genomic_DNA.
DR RefSeq; XP_658889.1; XM_653797.1.
DR AlphaFoldDB; Q5BDU5; -.
DR SMR; Q5BDU5; -.
DR STRING; 162425.CADANIAP00001335; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; EGL5A_EMENI; -.
DR CLAE; EGL5B_EMENI; -.
DR EnsemblFungi; CBF87793; CBF87793; ANIA_01285.
DR EnsemblFungi; EAA65878; EAA65878; AN1285.2.
DR GeneID; 2877061; -.
DR KEGG; ani:AN1285.2; -.
DR VEuPathDB; FungiDB:AN1285; -.
DR eggNOG; ENOG502QXN4; Eukaryota.
DR HOGENOM; CLU_029718_0_1_1; -.
DR InParanoid; Q5BDU5; -.
DR OMA; TDYIWPS; -.
DR OrthoDB; 722981at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IDA:UniProtKB.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
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 Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..326
FT /note="Endo-beta-1,4-glucanase A"
FT /id="PRO_5000049150"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CONFLICT 116
FT /note="Missing (in Ref. 1; BAA82592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 35812 MW; 7BFED0EF254B8D9F CRC64;
MRSLVLLSSV LALVAPSKGA FTWLGTNEAG AEFGEGSYPG ELGTEYIWPD LGTIGTLRNE
GMNIFRVAFS MERLVPDSLA GPVADEYFQD LVETVNGITA LGAYAVLDPH NYGRYYGNII
TSTDDFAAFW TILATEFASN ELVIFDTNNE YHTMDQSLVL NLNQAAIDAI RASGATSQYI
FAEGNSWTGA WTWVDVNDNM KALTDPQDKL IYEMHQYLDS DGSGTNTACV SSTIGSERVT
AATNWLRENG KLGVLGEFAG ANNQVCKDAV ADLLEYLEEN SDVWLGALWW AAGPWWGDYM
FNMEPTSGIA YQEYSEILQP YFVGSQ
