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Database: UniProt
Entry: R0HUK5_9BRAS
LinkDB: R0HUK5_9BRAS
Original site: R0HUK5_9BRAS 
ID   R0HUK5_9BRAS            Unreviewed;       846 AA.
AC   R0HUK5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CARUB_v10025350mg {ECO:0000313|EMBL:EOA29085.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA29085.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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         ECO:0000256|RuleBase:RU000675};
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   EMBL; KB870808; EOA29085.1; -; Genomic_DNA.
DR   RefSeq; XP_006296187.1; XM_006296125.1.
DR   AlphaFoldDB; R0HUK5; -.
DR   STRING; 81985.R0HUK5; -.
DR   GeneID; 17889760; -.
DR   KEGG; crb:17889760; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   OrthoDB; 5489808at2759; -.
DR   Proteomes; UP000029121; 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; 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:SF124; BETA-GALACTOSIDASE 2-RELATED; 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; PS50228; SUEL_LECTIN; 1.
PE   3: Inferred from homology;
KW   Apoplast {ECO:0000256|ARBA:ARBA00022523};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..846
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004341953"
FT   DOMAIN          760..846
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   846 AA;  92354 MW;  3224107AD947F14F CRC64;
     MVKGKRKMEM MLLLILQIVV AATAANVTYD HRALVIDGKR KILISGSIHY PRSTPEMWPD
     LIQKSKDGGL DVIETYVFWS GHEPEKNKYN FEGRYDLVKF VKLAAKAGLY VHLRIGPYVC
     AEWNYGGFPV WLHFVPGIKF RTDNEPFKAE MQRFTTKIVD LMKQEKLYAS QGGPIILSQI
     ENEYGNIASA YGAAGKSYIK WSASMALSLD TGVPWNMCQQ ADAPEPMINT CNGFYCDQFT
     PNSNNKPKMW TENWSGWFLG FGDPSPYRPV EDLAFAVARF YQRGGTFQNY YMYHGGSNFD
     RTSGGPLIST SYDYDAPIDE YGLLRQPKWG HLRDLHKAIK LCEDSLIATD PTITSLGSNL
     EAAVYKTSGS CAAFLANVGT KSDATVVFNG QSYVLPAWSV SILPDCKNVA FNTAKKNAAT
     ESTTFAPQSL KPDGGSSAEL GSQWSYIKEP IGISKTDAFL KPGLLEQINT TADKSDYLWY
     SLRMDIKGDE TFLDEGSKAV LHIESIGQVV YAFINGKLAG SGHDKQKISL VIPINLVPGK
     NTIDLLSVTV GLANYGPFFD LVGAGITGPV TLKSAKSGSS IDLATQQWTY QVGLKGEDTG
     LATGDSSEWV SKSPLPTKQP LIWYKTTFNA PSGSEPVAID FTGTGKGIAW VNGQSIGRYW
     PTSIAANNGC TDSCDYRGSY TAKKCVKNCG KPSQTLYHVP RSWLNPSGNT LVLLEEMGGD
     PTQISFATKQ TGSSLCLTVS QSHPPPVDTW TSDSKISNKH RTRPVLSLKC PVSTHVITSI
     KFASFGTPKG TCGSFTYGHC SSSRSLSLVQ KACIGLRSCN VEVSTRVFGE PCRGVVKSLA
     VEASCS
//
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