BG1_ARATH
ID BG1_ARATH Reviewed; 340 AA.
AC Q9M2M0; A0MF30; Q8LG04;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable glucan endo-1,3-beta-glucosidase BG1 {ECO:0000305};
DE EC=3.2.1.39 {ECO:0000305};
DE AltName: Full=Beta-1,3-glucanase 1 {ECO:0000305};
DE Short=AtBG1 {ECO:0000305};
DE Flags: Precursor;
GN Name=BG1 {ECO:0000305};
GN OrderedLocusNames=At3g57270 {ECO:0000312|Araport:AT3G57270};
GN ORFNames=F28O9.120 {ECO:0000312|EMBL:CAB68133.1};
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=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 [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].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in plant defense against pathogens.
CC {ECO:0000250|UniProtKB:F4J270}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P33157}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28605.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL137080; CAB68133.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79634.1; -; Genomic_DNA.
DR EMBL; DQ446773; ABE66024.1; -; mRNA.
DR EMBL; DQ653155; ABK28605.1; ALT_SEQ; mRNA.
DR EMBL; AY084537; AAM61105.1; -; mRNA.
DR PIR; T45805; T45805.
DR RefSeq; NP_191286.1; NM_115587.2.
DR AlphaFoldDB; Q9M2M0; -.
DR SMR; Q9M2M0; -.
DR STRING; 3702.AT3G57270.1; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR SwissPalm; Q9M2M0; -.
DR PaxDb; Q9M2M0; -.
DR PRIDE; Q9M2M0; -.
DR ProteomicsDB; 240822; -.
DR EnsemblPlants; AT3G57270.1; AT3G57270.1; AT3G57270.
DR GeneID; 824894; -.
DR Gramene; AT3G57270.1; AT3G57270.1; AT3G57270.
DR KEGG; ath:AT3G57270; -.
DR Araport; AT3G57270; -.
DR TAIR; locus:2082568; AT3G57270.
DR eggNOG; ENOG502QQ3M; Eukaryota.
DR HOGENOM; CLU_024953_0_0_1; -.
DR InParanoid; Q9M2M0; -.
DR OMA; GNEVMPG; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q9M2M0; -.
DR BioCyc; ARA:AT3G57270-MON; -.
DR PRO; PR:Q9M2M0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2M0; baseline and differential.
DR Genevisible; Q9M2M0; AT.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR044965; Glyco_hydro_17_plant.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR32227; PTHR32227; 1.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE 2: Evidence at transcript level;
KW Glycosidase; Hydrolase; Plant defense; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..340
FT /note="Probable glucan endo-1,3-beta-glucosidase BG1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434696"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CONFLICT 24
FT /note="G -> V (in Ref. 4; AAM61105)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="R -> G (in Ref. 4; AAM61105)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="V -> I (in Ref. 4; AAM61105)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> F (in Ref. 4; AAM61105)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="T -> V (in Ref. 4; AAM61105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 37655 MW; 7C9F913F979D2FE6 CRC64;
MDLRFLASLT LLLGLFFVNT NPTGGQVGVC YGRNGNNLPS PAETIALFKQ KNIQRVRLYS
PDHDVLAALR GSNIEVTLGL PNSYLQSVAS SQSQANAWVQ TYVMNYANGV RFRYISVGNE
VKISDSYAQF LVPAMENIDR AVLAAGLGGR IKVSTSVDMG VLRESYPPSK GSFRGDVMVV
MEPIIRFLVS KNSPLLLNLY TYFSYAGNVG QIRLDYALFT APSGIVSDPP RSYQNLFDAM
LDAMYSALEK SGGASLEIVV AETGWPTGGG TDTNIENARI YNNNLIKHVK NGTPKRPGKE
IETYLFAIYD ENQKPTPPYV EKFWGLFYPN KQPKYDINFY
