GenomeNet

Database: UniProt
Entry: BGA11_ARATH
LinkDB: BGA11_ARATH
Original site: BGA11_ARATH 
ID   BGA11_ARATH             Reviewed;         845 AA.
AC   Q9SCV1; O49609;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 122.
DE   RecName: Full=Beta-galactosidase 11;
DE            Short=Lactase 11;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   Name=BGAL11; OrderedLocusNames=At4g35010; ORFNames=M4E13.70;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gy I., Kreis M., Lecharny A.;
RT   "The beta-galactosidases are encoding by a multigene family in
RT   Arabidopsis thaliana.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17466346; DOI=10.1016/j.phytochem.2007.03.021;
RA   Ahn Y.O., Zheng M., Bevan D.R., Esen A., Shiu S.-H., Benson J.,
RA   Peng H.-P., Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C.;
RT   "Functional genomic analysis of Arabidopsis thaliana glycoside
RT   hydrolase family 35.";
RL   Phytochemistry 68:1510-1520(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA17766.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80218.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AJ270307; CAB64747.1; -; mRNA.
DR   EMBL; AL022023; CAA17766.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161586; CAB80218.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86446.1; -; Genomic_DNA.
DR   PIR; T05771; T05771.
DR   RefSeq; NP_567973.1; NM_119667.3.
DR   UniGene; At.706; -.
DR   ProteinModelPortal; Q9SCV1; -.
DR   SMR; Q9SCV1; -.
DR   STRING; 3702.AT4G35010.1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; Q9SCV1; -.
DR   PRIDE; Q9SCV1; -.
DR   EnsemblPlants; AT4G35010.1; AT4G35010.1; AT4G35010.
DR   GeneID; 829653; -.
DR   Gramene; AT4G35010.1; AT4G35010.1; AT4G35010.
DR   KEGG; ath:AT4G35010; -.
DR   Araport; AT4G35010; -.
DR   TAIR; locus:2131596; AT4G35010.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   HOGENOM; HOG000239919; -.
DR   InParanoid; Q9SCV1; -.
DR   OMA; PFRRDIR; -.
DR   OrthoDB; 179316at2759; -.
DR   PhylomeDB; Q9SCV1; -.
DR   BioCyc; ARA:AT4G35010-MONOMER; -.
DR   PRO; PR:Q9SCV1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SCV1; baseline and differential.
DR   Genevisible; Q9SCV1; AT.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005618; C:cell wall; IBA:GO_Central.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF02140; Gal_Lectin; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   2: Evidence at transcript level;
KW   Apoplast; Complete proteome; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    845       Beta-galactosidase 11.
FT                                /FTId=PRO_0000293093.
FT   DOMAIN      751    840       SUEL-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00260}.
FT   ACT_SITE    197    197       Proton donor. {ECO:0000255}.
FT   ACT_SITE    268    268       Nucleophile. {ECO:0000255}.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    269    269       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    300    300       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    395    395       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    752    752       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    784    784       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    814    814       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   845 AA;  95570 MW;  EAD24C68E0097B2D CRC64;
     MRKHSLDRWL LTAVLVVLLS SSSSFAAKKD AKKKKKSNKE VTYDGTSLII DGKRELLYSG
     SIHYPRSTPE MWPSIIKRAK QGGLNTIQTY VFWNVHEPQQ GKFNFSGRAD LVKFIKLIQK
     NGMYVTLRLG PFIQAEWTHG GLPYWLREVP GIFFRTDNKQ FKEHTERYVR MILDKMKEER
     LFASQGGPII LGQIENEYSA VQRAYKQDGL NYIKWASNLV DSMKLGIPWV MCKQNDAPDP
     MINACNGRHC GDTFPGPNRE NKPSLWTENW TTQFRVFGDP PTQRSVEDIA YSVARFFSKN
     GTHVNYYMYH GGTNFGRTSA HYVTTRYYDD APLDEYGLEK EPKYGHLKHL HNALNLCKKP
     LLWGQPKTEK PGKDTEIRYY EQPGTKTCAA FLANNNTEAA ETIKFKGREY VIAPRSISIL
     PDCKTVVYNT AQIVSQHTSR NFMKSKKANK KFDFKVFTET LPSKLEGNSY IPVELYGLTK
     DKTDYGWYTT SFKVHKNHLP TKKGVKTFVR IASLGHALHA WLNGEYLGSG HGSHEEKSFV
     FQKQVTLKAG ENHLVMLGVL TGFPDSGSYM EHRYTGPRGI SILGLTSGTL DLTESSKWGN
     KIGMEGEKLG IHTEEGLKKV EWKKFTGKAP GLTWYQTYFD APESVSAATI RMHGMGKGLI
     WVNGEGVGRY WQSFLSPLGQ PTQIEYHIPR SFLKPKKNLL VIFEEEPNVK PELMDFAIVN
     RDTVCSYVGE NYTPSVRHWT RKKDQVQAIT DNVSLTATLK CSGTKKIAAV EFASFGNPIG
     VCGNFTLGTC NAPVSKQVIE KHCLGKAECV IPVNKSTFQQ DKKDSCKNVV KMLAVQVKCG
     RGKKN
//
DBGET integrated database retrieval system