ID A0A3Q3SH13_9TELE Unreviewed; 651 AA.
AC A0A3Q3SH13;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 23.
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};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000024415.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000024415.2}
RP IDENTIFICATION.
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; A0A3Q3SH13; -.
DR STRING; 205130.ENSMAMP00000024415; -.
DR Ensembl; ENSMAMT00000025043.2; ENSMAMP00000024415.2; ENSMAMG00000016412.2.
DR GeneTree; ENSGT00950000182942; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
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; 1.
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:UP000261640};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..651
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030876821"
FT DOMAIN 37..352
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 399..510
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 540..601
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 184
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 651 AA; 72362 MW; 3EAC0C2C9DB95D4E CRC64;
MTSYKWFLIV FLISVVIIRI GLSAPRSFSV DYKSDCFRKD GEEFRYISGS IHYSRIPRVY
WKDRLLKMYM AGLNAIQTYI PWNYHEETPG LYNFSGDRDV EYFLKLAQDI GLLVILRPGP
YICAEWDMGG LPAWLLRKKD IVLRSSDPDY IAAVDKWMGK LLPMIQPFLY QNGGPIITVQ
VENEYGSYFA CDYNYLRHLL KLFRSHLGEQ VVLFTTDGAG INYLKCGSMQ DLYATVDFGP
GANVTAAFEV QRHAEPHGPL VNSEFYTGWL DHWGSPHSIV PSTAVAKSLN EILAVGANVN
LYMFIGGTNF GYWNGANALY DAQPTSYDYD APLTEAGDLT EKYFAIREVI NMYRKVPEGP
IPPSTPKYAY GAVQMKQLQT ITEALEKLSF SGPVKSTYPQ TFTELNQAFG YMLYRTILPV
NCSTPTPLSS PLNGVHDRAY VSVDGVPMGV LERNTATTVN VTGKAGSQVD MLVENMGRIN
YGKNINDFKG LVSNLTLGAD ILTGWTMYSL SIDEAVSQGL LGKKEPTSTD PPQPAALAPP
TFYGGSLIIP DGIPDLPQDT YIKLPKWKKG QVWINGFNLG RYWPARGPQV TLFVPANILS
TAAPNNVTVL ELEEAPCSSG PCTVEFTATA ILNATVHSDH RRLLSKEDLL S
//