BGA11_ORYSJ
ID BGA11_ORYSJ Reviewed; 848 AA.
AC Q6ZJJ0; A0A0P0XI61;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Beta-galactosidase 11;
DE EC=3.2.1.23;
DE AltName: Full=Lactase 115;
DE Flags: Precursor;
GN OrderedLocusNames=Os08g0549200, LOC_Os08g43570; ORFNames=OJ1479_B11.10;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; AP003912; BAD08952.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF24354.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06573.1; -; Genomic_DNA.
DR EMBL; AK069066; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015650676.1; XM_015795190.1.
DR AlphaFoldDB; Q6ZJJ0; -.
DR SMR; Q6ZJJ0; -.
DR STRING; 4530.OS08T0549200-01; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q6ZJJ0; -.
DR PRIDE; Q6ZJJ0; -.
DR EnsemblPlants; Os08t0549200-01; Os08t0549200-01; Os08g0549200.
DR GeneID; 4346248; -.
DR Gramene; Os08t0549200-01; Os08t0549200-01; Os08g0549200.
DR KEGG; osa:4346248; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_1_1; -.
DR InParanoid; Q6ZJJ0; -.
DR OMA; FEYHIPR; -.
DR OrthoDB; 179316at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; Q6ZJJ0; baseline and differential.
DR Genevisible; Q6ZJJ0; OS.
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; 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; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..848
FT /note="Beta-galactosidase 11"
FT /id="PRO_0000294163"
FT DOMAIN 750..837
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 560
FT /note="D -> N (in Ref. 4; AK069066)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="G -> R (in Ref. 4; AK069066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 848 AA; 94739 MW; 81C585356683BA05 CRC64;
MSAAAVLAVV AAAVAALAAA ASGYELTKNG TVITYDRRSL IIDGHREIFF SGSIHYPRSP
PDTWPDLISK AKEGGLNVIE SYVFWNGHEP EQGVYNFEGR YDLIKFFKLI QEKEMYAIVR
IGPFVQAEWN HGGLPYWLRE IPDIIFRTNN EPFKKYMKQF VTLIVNKLKE AKLFASQGGP
IILAQIENEY QHLEVAFKEA GTKYINWAAK MAIATNTGVP WIMCKQTKAP GEVIPTCNGR
HCGDTWPGPA DKKKPLLWTE NWTAQYRVFG DPPSQRSAED IAFSVARFFS VGGTMANYYM
YHGGTNFGRN GAAFVMPRYY DEAPLDEFGL YKEPKWGHLR DLHHALRHCK KALLWGNPSV
QPLGKLYEAR VFEMKEKNVC VAFLSNHNTK EDGTVTFRGQ KYFVARRSIS ILADCKTVVF
STQHVNSQHN QRTFHFADQT VQDNVWEMYS EEKIPRYSKT SIRTQRPLEQ YNQTKDKTDY
LWYTTSFRLE TDDLPYRKEV KPVLEVSSHG HAIVAFVNDA FVGCGHGTKI NKAFTMEKAM
DLKVGVNHVA ILSSTLGLMD SGSYLEHRMA GVYTVTIRGL NTGTLDLTTN GWGHVVGLDG
ERRRVHSEQG MGAVAWKPGK DNQPLTWYRR RFDPPSGTDP VVIDLTPMGK GFLFVNGEGL
GRYWVSYHHA LGKPSQYLYH VPRSLLRPKG NTLMFFEEEG GKPDAIMILT VKRDNICTFM
TEKNPAHVRW SWESKDSQPK AVAGAGAGAG GLKPTAVLSC PTKKTIQSVV FASYGNPLGI
CGNYTVGSCH APRTKEVVEK ACIGRKTCSL VVSSEVYGGD VHCPGTTGTL AVQAKCSKRP
PRSAATAQ
