ID A0A3Q2KUG6_HORSE Unreviewed; 623 AA.
AC A0A3Q2KUG6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN Name=GLB1 {ECO:0000313|VGNC:VGNC:18367};
GN Synonyms=TMPPE {ECO:0000313|Ensembl:ENSECAP00000027822.2};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000027822.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000027822.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000027822.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000027822.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000027822.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans.
CC {ECO:0000256|ARBA:ARBA00002691}.
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|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR AlphaFoldDB; A0A3Q2KUG6; -.
DR STRING; 9796.ENSECAP00000027822; -.
DR PaxDb; 9796-ENSECAP00000027822; -.
DR Ensembl; ENSECAT00000037822.2; ENSECAP00000027822.2; ENSECAG00000011942.4.
DR VGNC; VGNC:18367; GLB1.
DR GeneTree; ENSGT00950000182942; -.
DR InParanoid; A0A3Q2KUG6; -.
DR OMA; RAHPDTW; -.
DR Proteomes; UP000002281; Chromosome 16.
DR Bgee; ENSECAG00000011942; Expressed in chorionic villus and 23 other cell types or tissues.
DR ExpressionAtlas; A0A3Q2KUG6; baseline.
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; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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:SF172; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 2.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
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:UP000002281};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..623
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040410001"
FT DOMAIN 40..355
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 398..476
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 510..571
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 267
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 623 AA; 69928 MW; DD45E6F137ECB477 CRC64;
MLGVVRFLSL LLVPLLLGSA RGLRNASQRT FKIDYSHNRF LKDGQPFRYI SGSIHYFRIP
RFYWKDRLLK MKMAGLNAIQ TYVPWNFHEP QPGQYQFSED HDVEYFIQLA HELGLLVILR
PGPYICAEWD MGGLPAWLLE KQSIVLRSSD PDYLAAVDKW LGVLLPKMKP LLYQNGGPII
TVQVENEYGS YFTCDYDYLR FLQKLFHQHL GDDVLLFTTD GIFQKFLKCG ALQGLYATVD
FGSGINVTAA FQIQRKSEPR GPLINSEFYT GWLDHWGQRH SKAKTDVVAS TLYDILASGA
NVNMYMFIGG TNFAYWNGAN LPYQPQPTSY DYDAPLSEAG DLTEKYFALR DVIKKFEKVP
EGFIPPSTPK FAYGKVAMKK LKTVEGALDI LCPAGPIKSL YPLTFIQVKQ VPQGILERNT
VTTLNITGKA GATLDLLVEN MGRINYGTYI NDSKGLISNL TLGSKILTDW MIFPLDTEDA
VSSHLGGWDG HDSGSRDEAC ACNSSNYTLP AFYVGNFSIP SGISDLPQDT FIRFPGWTKG
QVWINGFNLG RYWPARGPQM TLFVPQHILM TSAPNSVIVL ELEYAPCSDN NLELCAVEFV
DRPDIGASQT QSRLPPHLSI QGL
//