BGL05_ARATH
ID BGL05_ARATH Reviewed; 500 AA.
AC Q8RXN9; F4IER4; O80749;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Putative beta-glucosidase 5;
DE Short=AtBGLU5;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU5; OrderedLocusNames=At1g60260; ORFNames=T13D8.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
RA Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
RA Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.;
RT "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT family 1.";
RL Plant Mol. Biol. 55:343-367(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RXN9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RXN9-2; Sequence=VSP_040524;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to introns retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24061.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC24061.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC004473; AAC24061.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33671.2; -; Genomic_DNA.
DR EMBL; AY080772; AAL87256.1; -; mRNA.
DR PIR; T02278; T02278.
DR RefSeq; NP_001319275.1; NM_001333890.1.
DR AlphaFoldDB; Q8RXN9; -.
DR SMR; Q8RXN9; -.
DR STRING; 3702.AT1G60260.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q8RXN9; -.
DR PRIDE; Q8RXN9; -.
DR GeneID; 3767578; -.
DR KEGG; ath:AT1G60260; -.
DR Araport; AT1G60260; -.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q8RXN9; -.
DR OrthoDB; 408001at2759; -.
DR BioCyc; ARA:AT1G60260-MON; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RXN9; baseline and differential.
DR Genevisible; Q8RXN9; AT.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 5: Uncertain;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..500
FT /note="Putative beta-glucosidase 5"
FT /id="PRO_0000389567"
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT ACT_SITE 394
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 434
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 441..442
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 205..212
FT /evidence="ECO:0000250"
FT VAR_SEQ 284..500
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040524"
FT CONFLICT 184
FT /note="I -> V (in Ref. 3; AAL87256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 56645 MW; 2F6ECBC2A0607D5B CRC64;
MEQFFALFTI FLSFAFPGRC SDVFSRSDFP EGFLFGAGTS AYQWEGAAAE DGRKPSVWDT
LCYSRNIGNG DVTCDGYHKY KEDVKLMVDT NLDAFRFSIS WSRLIPNGRG SVNQKGLQFY
KNLISELITH GIEPHVTLYH YDHPQYLEDE YGGWVNNMMI KDFTAYVDVC FREFGNYVKF
WTTINEANVF TIGGYNDGDT PPGRCSLPGK NCLLGNSSTE TYIVGHNLLL AHASASRLYK
QKYKDKQGGS IGFGLYLMGL TPSTSSKDDA IATQRAKDFY FGWFLGPLIF GDYPDTMKRT
IGSRLPVFSE EESEQVKGSS DFIGINHYFA ASVTNIKFKP SISGNPDFYS DMGAYVTYLG
NFSVIEYPVA PWTMEAVLEY IKQSYDNPPV YILENGTPMT QHKDTHRVEY MNAYIGGVLK
SIRNGSDTRG YFVWSFMDLF ELIGRYDYGY GLYSVNFSDP HRKRSPRLSA HWYSDFLKGK
TSFLDSKGIK ELQSNFSSSS
