ID A0A2P5CTX8_PARAD Unreviewed; 848 AA.
AC A0A2P5CTX8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=PanWU01x14_123860 {ECO:0000313|EMBL:PON64509.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON64509.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PON64509.1}.
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DR EMBL; JXTB01000095; PON64509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5CTX8; -.
DR STRING; 3476.A0A2P5CTX8; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
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; IPR025300; BetaGal_jelly_roll_dom.
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:SF88; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000237105};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..848
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015185775"
FT DOMAIN 761..847
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 848 AA; 93586 MW; 917F1AD0174D9543 CRC64;
MASLGSTSTR NHEILILIAM SLAPLLTLCS EAAPATTDNN VSYDAKSFII NGERRLIFSG
SIHYPRSTEQ MWPDLIQKAK EGGLDAIETY IFWDRHEPVR RHYDFSGNLD FVKFFKTIQE
AGLYGVLRIG PYVCAEWSYG GFPLWLKNMP GIQLRTNNEI YKNEMQTFVT KIVNMCKEAK
LFASQGGPII IAQIENEYGN IMGPYGEAGK AYINWCAQMA VSQNTGVPWI MCQQNDAPEP
MINTCNGYYC DWFTPNNPNS PKMFTENWVG WFKKWGERDP HRTAEDVAYS VARFFQRGGV
FNNYYMYHGG TNFGRTAGGP YIATSYDYDA PLDEYGNLNQ PKWGHLKRLH EAIKVGEKIL
TTGNWTGKEI FPGVNLTTYT DVVTGQRFCF LSNTNNSGDP ITVDLQNDGV YWLPAWSVSI
LDGCNKEIYN TAKVNSQTSL YVKKQSSQHL NHNSHKGNDK LTWLWAPEDI KDTLRGKGRF
RASQLLDQKL TTSDVSDYLW YMTTVAVNKT QSLTLSVKAA GHVLHVYVNK KYVGSHLGTA
GQLGFTFESP VVLSRGENTI TLLSATVGLP NYGAFYDSGP TGIVGGPVLL IRNDNSTPND
LSFNQWSYKV GLNGEAKRFF DPTSSRAPWR TSKSNELPTG RRMTWYKASF QTPSGDEPVV
VDLLGMGKGH AWVNGHSLGR IWPSVLADSN GCGGDCDYRG DYNPGKCPTN CGNSSQRSYH
VPRAFLNVGK TNTLILFEEL GGNPQGVSFQ TVSVETVCGN AYEGSMLELS CHGGKTISGI
DFASFGNPVG KCGSFSKGSC ESKVSISEVE KACVGKEACA IVVSDGTFGS TSCGNVTKRL
AVQASCEN
//
