GenomeNet

Database: UniProt
Entry: BGA15_ARATH
LinkDB: BGA15_ARATH
Original site: BGA15_ARATH 
ID   BGA15_ARATH             Reviewed;         779 AA.
AC   Q9C6W4; F4IAX4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   13-FEB-2019, entry version 112.
DE   RecName: Full=Beta-galactosidase 15;
DE            Short=Lactase 15;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   Name=BGAL15; OrderedLocusNames=At1g31740; ORFNames=F27M3.5;
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 [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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16267099; DOI=10.1093/pcp/pci223;
RA   Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G.,
RA   Zarra I.;
RT   "Apoplastic glycosidases active against xyloglucan oligosaccharides of
RT   Arabidopsis thaliana.";
RL   Plant Cell Physiol. 47:55-63(2006).
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   -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in roots and
CC       siliques. {ECO:0000269|PubMed:16267099}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
DR   EMBL; AC074360; AAG60136.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31387.2; -; Genomic_DNA.
DR   RefSeq; NP_001319124.1; NM_001332978.1.
DR   ProteinModelPortal; Q9C6W4; -.
DR   SMR; Q9C6W4; -.
DR   STRING; 3702.AT1G31740.1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; Q9C6W4; -.
DR   PRIDE; Q9C6W4; -.
DR   EnsemblPlants; AT1G31740.1; AT1G31740.1; AT1G31740.
DR   GeneID; 840061; -.
DR   Gramene; AT1G31740.1; AT1G31740.1; AT1G31740.
DR   KEGG; ath:AT1G31740; -.
DR   Araport; AT1G31740; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   InParanoid; Q9C6W4; -.
DR   OMA; CEASNNA; -.
DR   OrthoDB; 179316at2759; -.
DR   PhylomeDB; Q9C6W4; -.
DR   BioCyc; ARA:AT1G31740-MONOMER; -.
DR   PRO; PR:Q9C6W4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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     19       {ECO:0000255}.
FT   CHAIN        20    779       Beta-galactosidase 15.
FT                                /FTId=PRO_0000293094.
FT   DOMAIN      694    779       SUEL-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00260}.
FT   ACT_SITE    178    178       Proton donor. {ECO:0000255}.
FT   ACT_SITE    247    247       Nucleophile. {ECO:0000255}.
FT   CARBOHYD    148    148       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    248    248       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    345    345       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    374    374       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    489    489       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    495    495       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    555    555       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   779 AA;  86342 MW;  888813DF318890B0 CRC64;
     MVSLSFILCC VLVSSCAYAT IVSHDGRAIT IDGHRRVLLS GSIHYPRSTT EMWPDLIKKG
     KEGSLDAIET YVFWNAHEPT RRQYDFSGNL DLIRFLKTIQ NEGMYGVLRI GPYVCAEWNY
     GGFPVWLHNM PGMEFRTTNT AFMNEMQNFT TMIVEMVKKE KLFASQGGPI ILAQIENEYG
     NVIGSYGEAG KAYIQWCANM ANSLDVGVPW IMCQQDDAPQ PMLNTCNGYY CDNFSPNNPN
     TPKMWTENWT GWYKNWGGKD PHRTTEDVAF AVARFFQKEG TFQNYYMYHG GTNFDRTAGG
     PYITTTYDYD APLDEFGNLN QPKYGHLKQL HDVLHAMEKT LTYGNISTVD FGNLVTATVY
     QTEEGSSCFI GNVNETSDAK INFQGTSYDV PAWSVSILPD CKTETYNTAK INTQTSVMVK
     KANEAENEPS TLKWSWRPEN IDSVLLKGKG ESTMRQLFDQ KVVSNDESDY LWYMTTVNLK
     EQDPVLGKNM SLRINSTAHV LHAFVNGQHI GNYRVENGKF HYVFEQDAKF NPGANVITLL
     SITVGLPNYG AFFENFSAGI TGPVFIIGRN GDETIVKDLS THKWSYKTGL SGFENQLFSS
     ESPSTWSAPL GSEPVVVDLL GLGKGTAWIN GNNIGRYWPA FLSDIDGCSA EYHVPRSFLN
     SEGDNTLVLF EEIGGNPSLV NFQTIGVGSV CANVYEKNVL ELSCNGKPIS AIKFASFGNP
     GGDCGSFEKG TCEASNNAAA ILTQECVGKE KCSIDVSEDK FGAAECGALA KRLAVEAIC
//
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