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 25-MAY-2022, entry version 90.
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 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 [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 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).
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 enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:19585695}. Note=Covalently-linked to the cell wall.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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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 AlphaFoldDB; Q5BD29; -.
DR SMR; Q5BD29; -.
DR STRING; 162425.CADANIAP00008179; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR EnsemblFungi; CBF85093; CBF85093; ANIA_01551.
DR EnsemblFungi; EAA64258; EAA64258; AN1551.2.
DR GeneID; 2874885; -.
DR KEGG; ani:AN1551.2; -.
DR VEuPathDB; FungiDB:AN1551; -.
DR eggNOG; ENOG502QS0R; Eukaryota.
DR HOGENOM; CLU_027285_2_1_1; -.
DR InParanoid; Q5BD29; -.
DR OMA; VVCPYAT; -.
DR OrthoDB; 1142019at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
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;
KW Carbohydrate metabolism; Cell wall; Cellulose degradation; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..555
FT /note="Probable beta-glucosidase btgE"
FT /id="PRO_0000395136"
FT REGION 92..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 392
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 488
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
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
