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Database: UniProt
Entry: K3Z3X6_SETIT
LinkDB: K3Z3X6_SETIT
Original site: K3Z3X6_SETIT 
ID   K3Z3X6_SETIT            Unreviewed;       809 AA.
AC   K3Z3X6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
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};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL15371, ECO:0000313|Proteomes:UP000004995};
RN   [1] {ECO:0000313|EnsemblPlants:KQL15371, ECO:0000313|Proteomes:UP000004995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL15371,
RC   ECO:0000313|Proteomes:UP000004995};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EnsemblPlants:KQL15371}
RP   IDENTIFICATION.
RC   STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL15371};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) 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         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; AGNK02001696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K3Z3X6; -.
DR   EnsemblPlants; KQL15371; KQL15371; SETIT_021244mg.
DR   Gramene; KQL15371; KQL15371; SETIT_021244mg.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   InParanoid; K3Z3X6; -.
DR   OMA; INNWKAF; -.
DR   Proteomes; UP000004995; Chromosome III.
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   CDD; cd22842; Gal_Rha_Lectin_BGal; 1.
DR   Gene3D; 2.60.120.740; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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:SF190; BETA-GALACTOSIDASE 7; 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; 2.
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:UP000004995};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..809
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010969140"
FT   DOMAIN          723..809
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   809 AA;  90195 MW;  0B6791200B863B2A CRC64;
     MPINIAVLAV LATVCTPAAA AERRRWVEEG DGVRREVTLD SRALVVDGTR RVLFAGEMHY
     TRSTPEMWPR LIAKAKEGGL DVIQTYVFWN VHEPVQGQYN FEGRYDLVKF IKEIQAQGLY
     VSLRIGPFIE AEWKYGGFPF WLHDVPNITF RSDNEPFKQH MQRFVTDIVS MMKHEGLYYP
     QGGPIITSQI ENEYQMVEPA FGSSGQRYVR WAAAMAVNLQ TGVPWTMCKQ NDAPDPVVGI
     HSHTTTLNFH NYLIYGNDTK LRSPEDIAFA VALFIARKNG SYMSYYMYHG GTNFGRFSSS
     YVTTNYYDGA PLDEYGLIWQ PTWGHLRELH TAVKQSSEPL LFGTYSNFSL GQEQEAHIFE
     TESQCVAFLV NFDQHQISEV VFRNISLQLA PKSISILSDC KRVVFETAKV NAQHGSRTAE
     EVQSFSDINT WKAFKEPIPQ DVSKAMYTGN QLFDHLSTTK DETDYLWYIV GYEYTPSDDG
     QLVLINVESR AHILHAFVNN AYVGKNLIKH HGRIHGSHDG PASIILSTNI SLNEGPNNIS
     LLSAMVGSPD SGAHMERRVF GIRKVSIQQG QEPEHLLDNE LWGNQVGLFG ERNHIYTQEG
     SKSVEWTTIN NLAYSPLIWY KTTFPTPAGN DAIALNLTSM GKGEVWINGE SIGRYWVSFK
     APSGNPSQSL YHIPRQFLNP QDNILVLFEE MGGDPQQITV NTVSVTRVCS NVNELSAPSL
     QSQDNEPAVN LWCQEGKQIS AIEFASYGNP VGDCTNYGSG SCHAGSSDSV VKQACLGKSG
     CSIPVTTDKF GGDPCPGIQK SLVVVASCG
//
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