ID BGA16_ARATH Reviewed; 815 AA.
AC Q8GX69; Q9CAR2; Q9FVW7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=Beta-galactosidase 16;
DE Short=Lactase 16;
DE EC=3.2.1.23;
DE Flags: Precursor;
GN Name=BGAL16; OrderedLocusNames=At1g77410; ORFNames=F2P24.12, T5M16.1;
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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
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 expression levels in
CC siliques. {ECO:0000269|PubMed:16267099}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG29193.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAO64909.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC43014.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC010704; AAG51670.1; -; Genomic_DNA.
DR EMBL; AC078898; AAG29193.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35975.1; -; Genomic_DNA.
DR EMBL; AK118405; BAC43014.1; ALT_FRAME; mRNA.
DR EMBL; BT005974; AAO64909.1; ALT_FRAME; mRNA.
DR PIR; D96803; D96803.
DR RefSeq; NP_177866.2; NM_106391.2.
DR AlphaFoldDB; Q8GX69; -.
DR SMR; Q8GX69; -.
DR STRING; 3702.Q8GX69; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR GlyCosmos; Q8GX69; 12 sites, No reported glycans.
DR iPTMnet; Q8GX69; -.
DR PaxDb; 3702-AT1G77410-1; -.
DR ProteomicsDB; 240781; -.
DR EnsemblPlants; AT1G77410.1; AT1G77410.1; AT1G77410.
DR GeneID; 844078; -.
DR Gramene; AT1G77410.1; AT1G77410.1; AT1G77410.
DR KEGG; ath:AT1G77410; -.
DR Araport; AT1G77410; -.
DR TAIR; AT1G77410; BGAL16.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q8GX69; -.
DR OMA; EYGMVAR; -.
DR PhylomeDB; Q8GX69; -.
DR PRO; PR:Q8GX69; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GX69; baseline and differential.
DR Genevisible; Q8GX69; AT.
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 CDD; cd22842; Gal_Rha_Lectin_BGal; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR048913; BetaGal_gal-bd.
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:SF201; BETA-GALACTOSIDASE 16; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 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; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..815
FT /note="Beta-galactosidase 16"
FT /id="PRO_0000293095"
FT DOMAIN 729..815
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 252
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 815 AA; 91648 MW; 47B97FBC710A0508 CRC64;
MTTFQYSLVF LVLMAVIVAG DVANVTYDGR SLIIDGEHKI LFSGSIHYTR STPQMWPSLI
AKAKSGGIDV VDTYVFWNVH EPQQGQFDFS GSRDIVKFIK EVKNHGLYVC LRIGPFIQGE
WSYGGLPFWL HNVQGIVFRT DNEPFKYHMK RYAKMIVKLM KSENLYASQG GPIILSQIEN
EYGMVGRAFR QEGKSYVKWT AKLAVELDTG VPWVMCKQDD APDPLVNACN GRQCGETFKG
PNSPNKPAIW TENWTSFYQT YGEEPLIRSA EDIAFHVALF IAKNGSFVNY YMYHGGTNFG
RNASQFVITS YYDQAPLDEY GLLRQPKWGH LKELHAAVKL CEEPLLSGLQ TTISLGKLQT
AFVFGKKANL CAAILVNQDK CESTVQFRNS SYRLSPKSVS VLPDCKNVAF NTAKVNAQYN
TRTRKARQNL SSPQMWEEFT ETVPSFSETS IRSESLLEHM NTTQDTSDYL WQTTRFQQSE
GAPSVLKVNH LGHALHAFVN GRFIGSMHGT FKAHRFLLEK NMSLNNGTNN LALLSVMVGL
PNSGAHLERR VVGSRSVKIW NGRYQLYFNN YSWGYQVGLK GEKFHVYTED GSAKVQWKQY
RDSKSQPLTW YKASFDTPEG EDPVALNLGS MGKGEAWVNG QSIGRYWVSF HTYKGNPSQI
WYHIPRSFLK PNSNLLVILE EEREGNPLGI TIDTVSVTEV CGHVSNTNPH PVISPRKKGL
NRKNLTYRYD RKPKVQLQCP TGRKISKILF ASFGTPNGSC GSYSIGSCHS PNSLAVVQKA
CLKKSRCSVP VWSKTFGGDS CPHTVKSLLV RAQCS
//
