ID C5Z534_SORBI Unreviewed; 725 AA.
AC C5Z534;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=SORBI_3010G173800 {ECO:0000313|EMBL:EER88554.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER88554.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER88554.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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; CM000769; EER88554.1; -; Genomic_DNA.
DR RefSeq; XP_002437187.1; XM_002437142.1.
DR AlphaFoldDB; C5Z534; -.
DR STRING; 4558.C5Z534; -.
DR EnsemblPlants; EER88554; EER88554; SORBI_3010G173800.
DR GeneID; 8065029; -.
DR Gramene; EER88554; EER88554; SORBI_3010G173800.
DR KEGG; sbi:8065029; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; C5Z534; -.
DR OMA; YETWNIG; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000000768; Chromosome 10.
DR ExpressionAtlas; C5Z534; baseline and differential.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
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 PANTHER; PTHR23421:SF120; BETA-GALACTOSIDASE 9; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 2.
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.
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:UP000000768};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..725
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002961024"
FT DOMAIN 38..342
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 365..421
FT /note="Beta-galactosidase beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF17834"
FT DOMAIN 471..538
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT DOMAIN 617..703
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
SQ SEQUENCE 725 AA; 79149 MW; B225C42150F26543 CRC64;
MMSGGVLFLA LLAAAAALAI IVAPSPANAA VSYDHRAVVI NGQRRILISG SIHYPRSTPE
MWPDLLQKAK DGGLDVVQTY VFWNGHEPQQ GQYYFGDRYD LVRFVKLAKQ AGLFVHLRIG
PYVCAEWNFG GFPVWLKYVP GVSFRTDNAP FKAAMQAFVE KIVSMMKAEG LFEWQGGPII
LAQVENEYGP MESVMGGGAK PYANWAAKMA VATGAGVPWV MCKQDDAPDP VINTCNGFYC
DYFSPNSNSK PTMWTEAWTG WFTAFGGAVP HRPVEDMAFA VARFIQKGGS FVNYYMYHGG
TNFDRTSGGP FIATSYDYDA PIDEYGLLRQ PKWGHLRDLH KAIKQAEPAL VSGDPTIQTI
GNYEKAYVYK SSSGACAAFL SNYHTNAAAR VVFNGRRYDL PAWSISVLPD CRTAVFNTAT
VSSPSAPARM TPAGGFSWQS YSEATNSLDD RAFTKDGLVE QLSMTWDKSD YLWYTTYVNI
NSNEQFLKSG QWPQLTIYSA GHALQVFVNG QSYGAAYGGY DSPKLTYSGY VKMWQGSNKI
SILSAAVGLP NQGTHYEAWN VGVLGPVTLS GLNEGKRDLS NQKWTYQIGL HGESLGVHSV
AGSSSVEWGS AAGKQPLTWH KAYFNAPSGN APVALDMSSM GKGQAWVNGH HIGRYWSYKA
TGGSCGGCSY AGTYSETKCQ TGCGDVSQRY YHVPRSWLNP SGNLLVVLEE FGGDLSGVKL
VTRTT
//