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 03-AUG-2022, entry version 125.
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; 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 TISSUE SPECIFICITY.
RX PubMed=16267099; DOI=10.1093/pcp/pci223;
RA Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., 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., Peng H.-P.,
RA Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C.;
RT "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT family 35.";
RL Phytochemistry 68:1510-1520(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC 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. {ECO:0000305}.
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DR EMBL; AC074360; AAG60136.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31387.2; -; Genomic_DNA.
DR RefSeq; NP_001319124.1; NM_001332978.1.
DR AlphaFoldDB; Q9C6W4; -.
DR SMR; Q9C6W4; -.
DR STRING; 3702.AT1G31740.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q9C6W4; -.
DR PRIDE; Q9C6W4; -.
DR ProteomicsDB; 240857; -.
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 HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9C6W4; -.
DR OMA; YDNNKCV; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; Q9C6W4; -.
DR BioCyc; ARA:AT1G31740-MON; -.
DR PRO; PR:Q9C6W4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6W4; baseline and differential.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
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; 2.60.120.740; -; 1.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041392; GHD.
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 InterPro; IPR043159; Lectin_gal-bd_sf.
DR PANTHER; PTHR23421; PTHR23421; 1.
DR Pfam; PF13364; BetaGal_dom4_5; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF17834; GHD; 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; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..779
FT /note="Beta-galactosidase 15"
FT /id="PRO_0000293094"
FT DOMAIN 694..779
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 247
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="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
