(data stored in ACNUC16935 zone)

SWISSPROT: BTGE_EMENI

ID   BTGE_EMENI              Reviewed;         555 AA.
AC   Q5BD29; C8VMY9; Q1HFV1;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 76.
DE   RecName: Full=Probable beta-glucosidase btgE;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase btgE;
DE   AltName: Full=Cellobiase btgE;
DE   AltName: Full=Gentiobiase btgE;
DE   Flags: Precursor;
GN   Name=btgE; ORFNames=AN1551;
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].
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).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=19585695; DOI=10.1016/j.fgb.2008.07.022;
RA   de Groot P.W., Brandt B.W., Horiuchi H., Ram A.F., de Koster C.G.,
RA   Klis F.M.;
RT   "Comprehensive genomic analysis of cell wall genes in Aspergillus
RT   nidulans.";
RL   Fungal Genet. Biol. 46:S72-S81(2009).
CC   -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic
CC       enzymes involved in the degradation of cellulosic biomass.
CC       Catalyzes the last step releasing glucose from the inhibitory
CC       cellobiose (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-
CC       glucosyl residues with release of beta-D-glucose.
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:19585695}. Note=Covalently-linked to the cell
CC       wall.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family.
CC       {ECO:0000305}.
DR   EMBL; DQ490473; ABF50849.1; -; mRNA.
DR   EMBL; AACD01000025; EAA64258.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF85093.1; -; Genomic_DNA.
DR   RefSeq; XP_659155.1; XM_654063.1.
DR   ProteinModelPortal; Q5BD29; -.
DR   SMR; Q5BD29; -.
DR   STRING; 162425.CADANIAP00008179; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   EnsemblFungi; CADANIAT00008179; CADANIAP00008179; CADANIAG00008179.
DR   EnsemblFungi; EAA64258; EAA64258; AN1551.2.
DR   GeneID; 2874885; -.
DR   KEGG; ani:AN1551.2; -.
DR   HOGENOM; HOG000158427; -.
DR   InParanoid; Q5BD29; -.
DR   OMA; CPTPGTY; -.
DR   OrthoDB; EOG092C20DF; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q5BD29.
DR   SWISS-2DPAGE; Q5BD29.
KW   Carbohydrate metabolism; Cell wall; Cellulose degradation;
KW   Complete proteome; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    555       Probable beta-glucosidase btgE.
FT                                /FTId=PRO_0000395136.
FT   COMPBIAS     49    288       Thr-rich.
FT   ACT_SITE    488    488       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    546    546       Proton donor. {ECO:0000250}.
SQ   SEQUENCE   555 AA;  57672 MW;  B8F0DF0153079DCA CRC64;
     MRGAILATAA AFAGTAVADM HMRRHAHEGL HHRALHASSA VPEEECGCTT EVITYWGEPT
     TIPLSVPTST VTSETTETVH STSYSTVTVT ATSSAAPVET PSETPSPTPE VTLPTAGVTS
     YSETGTYTIP ATTITVTDTT TVCGATTTEL PSGTHTYGGV TTIVETATTI TCPYATVKPT
     GSTVTSVIET TTYVCPSAGT YTIAPTTTFV PTSTVVVYPT PETVTPGTYT NPGTTITVTR
     TEDVYVCPYT NGNVPTSVPA LPTTSAASTT TAVPSSSTTT SSATSVPTGA SGNKMGMTFT
     PYNNDGSCMA KNDVLEQVGL IKGKGFSHVR VYGTDCHTLE YVGAACSTHG LKMILGVNVE
     GSTGFDGARS QFKDITNWGQ WDLVSLIVVG NEVVTSNIAS AAQLASFVSE GASAFSAAGY
     TGQVTTAEPI DVWLSNGATL CPVVDILGAN LHPFFNPEFT AAEAGTLVSN QIKDLKQVCT
     GKDVINLETG WPNAGSANGK AIPGQSQQTT AIKSLVEKVG DVSVFFSYAD DGWKSKFATS
     DKYNVEQHWG CIDQF
//

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