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Database: UniProt
Entry: I1NTV5_ORYGL
LinkDB: I1NTV5_ORYGL
Original site: I1NTV5_ORYGL 
ID   I1NTV5_ORYGL            Unreviewed;       851 AA.
AC   I1NTV5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA01G0329500.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|Proteomes:UP000007306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA01G0329500.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00001412};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000256|ARBA:ARBA00004271}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   AlphaFoldDB; I1NTV5; -.
DR   STRING; 4538.I1NTV5; -.
DR   EnsemblPlants; ORGLA01G0329500.1; ORGLA01G0329500.1; ORGLA01G0329500.
DR   Gramene; ORGLA01G0329500.1; ORGLA01G0329500.1; ORGLA01G0329500.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   OMA; NGTHSPF; -.
DR   Proteomes; UP000007306; Unassembled WGS sequence.
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; 2.
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; 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:SF67; BETA-GALACTOSIDASE 10; 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; PS50228; SUEL_LECTIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..851
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003649061"
FT   DOMAIN          765..851
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   851 AA;  94624 MW;  5C0B84AE7753EA43 CRC64;
     MAGASSSFSL RRLLLLLLPL IPLLGATTAA AAGANSSVTY DQRSLIISGR RRLLISTSIH
     YPRSVPEMWP KLVAEAKDGG ADCVETYVFW NGHEPAQGQY YFEERFDLVR FAKIVKDAGL
     YMILRIGPFV AAEWTFGGVP VWLHYVPGTV FRTNNEPFKS HMKRFTTYIV DMMKKEQFFA
     SQGGHIILAQ VENEYGDMEQ AYGAGAKPYA MWAASMALAQ NTGVPWIMCQ QYDAPDPVIN
     TCNSFYCDQF KPNSPTKPKF WTENWPGWFQ TFGESNPHRP PEDVAFSVAR FFGKGGSLQN
     YYVYHGGTNF GRTTGGPFIT TSYDYDAPID EYGLRRLPKW AHLRDLHKSI KLGEHTLLYG
     NSSFVSLGPQ QEADVYTDQS GGCVAFLSNV DSEKDKVVTF QSRSYDLPAW SVSILPDCKI
     VAFNTAKVRS QTLMMDMVPA NLESSKVDGW SIFREKYGIW GNIDLVRNGF VDHINTTKDS
     TDYLWYTTSF DVDGSHLAGG NHVLHIESKG HAVQAFLNNE LIGSAYGNGS KSNFSVEMPV
     NLRAGKNKLS LLSMTVGLQN GGPMYEWAGA GITSVKISGM ENRIIDLSSN KWEYKIGLEG
     EYYSLFKADK GKDIRWMPQS EPPKNQPMTW YKVNVDVPQG DDPVGLDMQS MGKGLAWLNG
     NAIGRYWPRI SPVSDRCTSS CDYRGTFSPN KCRRGCGQPT QRWYHVPRSW FHPSGNTLVI
     FEEKGGDPTK ITFSRRTVAS VCSFVSEHYP SIDLESWDRN TQNDGRDAGK VQLSCPKGKS
     ISSVKFASFG NPSGTCRSYQ QGSCHHPNSI SVVEKACLNM NGCTVSLSDE GFGEDLCPGV
     TKTLAIEADC S
//
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