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BGL25_ARATH
ID   BGL25_ARATH             Reviewed;         531 AA.
AC   O82772;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Probable inactive beta-glucosidase 25;
DE            Short=AtBGLU25;
DE   Flags: Precursor;
GN   Name=BGLU25; Synonyms=GLUC; OrderedLocusNames=At3g03640; ORFNames=T12J13.8;
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 [GENOMIC DNA / MRNA].
RA   Gualberto J.M., Schell J., Palme K.;
RT   "Beta-glucosidase homolog.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
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   [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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved Glu residue involved in nucleophilic
CC       attack and essential for hydrolase activity. Its enzyme activity is
CC       therefore unsure. {ECO:0000305}.
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DR   EMBL; AF082157; AAC31962.1; -; mRNA.
DR   EMBL; AF082158; AAC32194.1; -; Genomic_DNA.
DR   EMBL; AC009327; AAF03468.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE73966.1; -; Genomic_DNA.
DR   PIR; T51956; T51956.
DR   RefSeq; NP_187014.1; NM_111235.4.
DR   AlphaFoldDB; O82772; -.
DR   SMR; O82772; -.
DR   STRING; 3702.AT3G03640.1; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PaxDb; O82772; -.
DR   PRIDE; O82772; -.
DR   ProteomicsDB; 240660; -.
DR   EnsemblPlants; AT3G03640.1; AT3G03640.1; AT3G03640.
DR   GeneID; 821201; -.
DR   Gramene; AT3G03640.1; AT3G03640.1; AT3G03640.
DR   KEGG; ath:AT3G03640; -.
DR   Araport; AT3G03640; -.
DR   TAIR; locus:2096449; AT3G03640.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; O82772; -.
DR   OMA; THQHSEN; -.
DR   OrthoDB; 408001at2759; -.
DR   PhylomeDB; O82772; -.
DR   BioCyc; ARA:AT3G03640-MON; -.
DR   PRO; PR:O82772; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; O82772; baseline and differential.
DR   Genevisible; O82772; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0019762; P:glucosinolate catabolic process; IBA:GO_Central.
DR   GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..531
FT                   /note="Probable inactive beta-glucosidase 25"
FT                   /id="PRO_0000389587"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         477..478
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        222..230
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   531 AA;  59807 MW;  18EF2E2FDCB7C23B CRC64;
     MALKAILFLG LFLVVIVSPI TVYGGAVCPA SSTFGRGSFP DGFLFGATTS AFQHEGAAEE
     GGRGSSIWDS FTLKQHSESN NNLDGRLGVD FYHHYKEDVQ LLKKLNMDAF RFSISWSRIF
     PHGKKDKGVS ETGVKFYNDL INELIANGVT PLVTLFQWDV PQALEDEYGG FLSDRILEDF
     RDFAQFAFNK YGDRVKHWVT INEPYEFSRG GYETGEKAPG RCSKYVNEKC VAGKSGHEVY
     TVSHNLLLAH AEAVEEFRKC GKCTGGKIGI VQSPMWFEPY DKKSTSSPSE EIVKRAMDFT
     LGWHMEPITH GDYPQAMKDV VGSRLPSFTP EQKEKLKGSY DFVGINYFTS TFVAHTDNVN
     PEKPSWEADS RLQLHSNNVD GFKIGSQPAT AKYPVCADGL RKVLKYIKEN YNDPEIIVTG
     NGYKETLEEK DVLPDALSDS NRKYYHMRHL MALHGAVCED KVNVKGYFVS SLMDGLEWED
     GYKTRSGLYY VDYGHNMGRH EKQSAKWLSK LLEKVPDTIQ SKVDSDSRKE L
 
 
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