ID A0A0D2NQE4_GOSRA Unreviewed; 843 AA.
AC A0A0D2NQE4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=B456_002G197200 {ECO:0000313|EMBL:KJB15808.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB15808.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB15808.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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; CM001741; KJB15808.1; -; Genomic_DNA.
DR RefSeq; XP_012467564.1; XM_012612110.1.
DR AlphaFoldDB; A0A0D2NQE4; -.
DR EnsemblPlants; KJB15808; KJB15808; B456_002G197200.
DR GeneID; 105785912; -.
DR Gramene; KJB15808; KJB15808; B456_002G197200.
DR KEGG; gra:105785912; -.
DR eggNOG; KOG0496; Eukaryota.
DR OrthoDB; 1204541at2759; -.
DR Proteomes; UP000032304; Chromosome 2.
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:SF52; BETA-GALACTOSIDASE 14; 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 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:UP000032304};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..843
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002247883"
FT DOMAIN 755..843
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 843 AA; 94905 MW; B7AF123EC5059EC3 CRC64;
MVEPRRLLMI FFLSTLLIAY SNANVEEIQK DTEEGDEEGK VGGQKAQGVT YDARSLIING
KRELLFSGAI HYPRSTPDMW PDLIKKAKQG GINTIETYVF WNGHEPVEGQ YNFEGEFDLV
KFIKLIHEHK LYAVVRVGPF IQAEWNHGGL PYWLREVPGI IFRSDNEPFK KHMKRFVTMI
VDKLKQEKLF APQGGPIILA QIENEYNTIQ RAFREKGDSY VQWAGKLALS LNANVPWIMC
KQRDAPDPVI NTCNGRHCGD TFYGPNKRNK PALWTENWTA QYRVFGDPPS QRSAEDLAYS
VARFFSKNGS MVNYYMYYGG TNFGRTSASF TTTRYYDEAP LDEFGLQREP KWGHLKDVHR
ALSLCKRALF WGVPTTLKLG PDQQAIVWQQ PGTSACAAFL ANNNTRLAQH VNFRGQDICL
PARSISVLPD CKTVVFNTQL VTTQHNSRNF VRSEIANKNF NWEMYREVPP VGLGFKFDVP
RELFHLTKDT TDYAWYTTSL KLGRRDLPMK KNVSPVLRVA SLGHGIHAYV NGEYAGSAHG
SKVEKSFVFQ RAVSLKEGEN HIALLGYLVG LPDSGAYMEK RFAGPRSITI LGLNTGTLDI
SQNGWGHQVG IDGEKKKLFT EEGSKSVQWT KPDQGGPLTW YKGYFDAPEG DNPVAIVMTG
MGKGMVWING RSIGRYWNNY LSPLKKPTQS EYHIPRAYLK PKNLIVLLEE EEGNPKDVHI
VTVNRDTICS AVSEIHPPSP RLFETKNGTL QPKVNDLKPR AELICPGKKQ IVAVEFASYG
DPFGACGAYF IGNCTAPESK QVVEKYCLGK PSCQIPLDSI HFSDQNGACT HLRKTLAVQV
KCA
//
