(data stored in ACNUC16935 zone)

SWISSPROT: EGLD_EMENI

ID   EGLD_EMENI              Reviewed;         357 AA.
AC   Q5BCX8; C8VN99; Q1HFV0;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 82.
DE   RecName: Full=Endo-beta-1,4-glucanase D;
DE            Short=Endoglucanase D;
DE            EC=3.2.1.4;
DE   AltName: Full=Carboxymethylcellulase D;
DE   AltName: Full=Cellulase D;
DE   Flags: Precursor;
GN   Name=eglD; ORFNames=AN1602;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   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
RT   enzymes 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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Has endoglucanase activity on substrates containing
CC       beta-1,4 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: Endohydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is under 6.0. {ECO:0000269|PubMed:16844780};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: Has a modular structure: an endo-beta-1,4-glucanase
CC       catalytic module at the N-terminus, a linker rich in serines and
CC       threonines, and a C-terminal carbohydrate-binding module (CBM).
CC       The genes for catalytic modules and CBMs seem to have evolved
CC       separately and have been linked by gene fusion.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family.
CC       {ECO:0000305}.
DR   EMBL; DQ490474; ABF50850.1; -; mRNA.
DR   EMBL; AACD01000026; EAA64722.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF85202.1; -; Genomic_DNA.
DR   RefSeq; XP_659206.1; XM_654114.1.
DR   ProteinModelPortal; Q5BCX8; -.
DR   SMR; Q5BCX8; -.
DR   STRING; 162425.CADANIAP00008239; -.
DR   CAZy; AA9; Auxiliary Activities 9.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   mycoCLAP; PMO9A_EMENI; -.
DR   EnsemblFungi; CADANIAT00008239; CADANIAP00008239; CADANIAG00008239.
DR   EnsemblFungi; EAA64722; EAA64722; AN1602.2.
DR   GeneID; 2875535; -.
DR   KEGG; ani:AN1602.2; -.
DR   HOGENOM; HOG000158937; -.
DR   InParanoid; Q5BCX8; -.
DR   KO; K19356; -.
DR   OMA; LTFEWYH; -.
DR   OrthoDB; EOG092C48ID; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IDA:UniProtKB.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR005103; Glyco_hydro_61.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF03443; Glyco_hydro_61; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q5BCX8.
DR   SWISS-2DPAGE; Q5BCX8.
KW   Carbohydrate metabolism; Cellulose degradation; Complete proteome;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    357       Endo-beta-1,4-glucanase D.
FT                                /FTId=PRO_0000394067.
FT   DOMAIN      319    355       CBM1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00597}.
FT   REGION       19    234       Catalytic.
FT   REGION      235    318       Ser/Thr-rich linker.
FT   ACT_SITE    163    163       Proton donor. {ECO:0000250}.
FT   ACT_SITE    209    209       Nucleophile. {ECO:0000250}.
FT   DISULFID    327    344       {ECO:0000250}.
FT   DISULFID    338    354       {ECO:0000250}.
SQ   SEQUENCE   357 AA;  36732 MW;  64BAB1984CDB49BD CRC64;
     MKFSSVLALA ASAKLVASHA TVFAVWINDE DQGLGNTADG YIRTPPNNSP VTDVTSTDLT
     CNVNGDQAAA KTLEVAAGDK ITFEWHHNSR DSSDDIIADS HKGPVLVYMA PTEAGSAGKN
     WVKIYEDGYN DGTWAVDTLI ANKGKHSVTV PDVPAGNYLF RPEIIALHEG NREGGAQLYM
     ECVQFKVTSD GTTQLPEGVS LPGAYTATDE GILFDIYSSF DSYPIPGPAV WDGASSGSGS
     SGSGSSSSAA ATSSAEKTAT STTAAATTTA VATSTSSATQ VQPTSVATFT TSVRPTTSAA
     PTTSAPTSSA APTGGTGTGS IQIYQQCGGM NYKGATGCAS GLTCKQWNPY YHQCVQA
//

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