ID BGLK_EMENI Reviewed; 838 AA.
AC Q5BA18; C8VKN4; Q1HFU3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 06-MAR-2013, entry version 55.
DE RecName: Full=Probable beta-glucosidase K;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase K;
DE AltName: Full=Cellobiase K;
DE AltName: Full=Gentiobiase K;
GN Name=bglK; ORFNames=AN2612;
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; Trichocomaceae; Emericella.
OX NCBI_TaxID=227321;
RN [1]
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 [2]
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: 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).
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 (By similarity).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC -!- SIMILARITY: Contains 1 PA14 domain.
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DR EMBL; DQ490481; ABF50857.1; -; mRNA.
DR EMBL; AACD01000043; EAA64717.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF87201.1; -; Genomic_DNA.
DR RefSeq; XP_660216.1; XM_655124.1.
DR ProteinModelPortal; Q5BA18; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblFungi; CADANIAT00009350; CADANIAP00009350; CADANIAG00009350.
DR GeneID; 2874655; -.
DR KEGG; ani:AN2612.2; -.
DR eggNOG; COG1472; -.
DR HOGENOM; HOG000031215; -.
DR OMA; YGEGVMV; -.
DR OrthoDB; EOG43FM52; -.
DR UniPathway; UPA00696; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 2.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR026892; Glyco_hydro_3.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR011658; PA14.
DR PANTHER; PTHR30620; PTHR30620; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF52279; Glyco_hydro_3_C; 1.
DR SUPFAM; SSF51445; Glyco_hydro_cat; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cellulose degradation; Complete proteome;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted.
FT CHAIN 1 838 Probable beta-glucosidase K.
FT /FTId=PRO_0000394898.
FT DOMAIN 406 553 PA14.
FT ACT_SITE 232 232 By similarity.
FT CARBOHYD 19 19 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 324 324 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 489 489 N-linked (GlcNAc...) (Potential).
SQ SEQUENCE 838 AA; 91126 MW; D69D1188267FB44C CRC64;
MGEISPRGGD FDIDYILENA SSLEKISLLA GHDFWHTAPL PRFNVPSVRV SDGPNGVRGT
KFFDGVRAAC LPCGTGLAAT WDQSLLFDAG VLIGQECLAK GAHCWLGPTV CIQRSPLGGR
GFESFAEDPY ATGKLAAAYI RGAQSTGVIS TIKHFAANDQ EHERISVNAV MSERALREVH
LLPFQIAIAD AAPGAVMTCY NKINGQHVSE SKEMLDGLLR KEWGWKGLIM SDWFGTYSTA
EALNAGLDLE MPGPTRLRGP LLELAISSRK VSRSTLDERA RTVLEFVKRA NKAEVSTVES
TRDFPEDRRL NRKLAADSIV LLKNESGLLP LNLKALKSAA LIGPNMKTAA FCGGGSASLQ
PYYSISPYQG IMNQLPPGVE IIYETGASSY VFIPELEASE VRTPEGQPGL RMRFYREPPS
VKERRVVEET ILQESSWQLM GFSNPQLDRL FYADIEAELI APATGPFEFG LAVYGSGSLF
IDDQLIIDNT TVQRGGNFFF GKGTREEKAT VDLVKGQLYK IRVEFASGPS SKLMKPGVVN
FGGGAGRLGM VQAIDPELAI ARAVEAAKRA DVTILGVGLT RDHESEGFDR SHMDLPPAVA
SLVTAVLDVA PDAILMTQSG TPFNMLPWAD NVKTHLHAWF GGNELGNGIA DVLFGVVNPS
GKLPLSFPRR IEDTPTYLNF GSERGQVTYG EGIYVGYRYY EKVLRDVLYP FGHGLSYTSF
AYSDFAVDTA SATLNVRNSG DVAGAEVVQL YIAADATTSS IARPVKELKG FAKVTLQPGE
TCSVSIPFDR FTTAFWDQEA HVWTCEKGQY RVMVGSSSQN ILLEGVLEIK ETTTWSGL
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