ID A0A3L8SY13_CHLGU Unreviewed; 676 AA.
AC A0A3L8SY13;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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};
DE Flags: Fragment;
GN ORFNames=DV515_00001729 {ECO:0000313|EMBL:RLW11391.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW11391.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW11391.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW11391.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW11391.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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}.
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:RLW11391.1}.
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DR EMBL; QUSF01000003; RLW11391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SY13; -.
DR STRING; 44316.ENSEGOP00005003492; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
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; 2.
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:UP000276834};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..676
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017980137"
FT DOMAIN 33..348
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 395..448
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 465..532
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 561..622
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 180
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RLW11391.1"
SQ SEQUENCE 676 AA; 76500 MW; CE4D3702BE9C67B3 CRC64;
LKKLYCVFFV LFCFCVQNVP ERSFGIDYDS NCFVKDGKPF RYISGSIHYS RVPSYYWKDR
LLKMKMAGLD AIQTYVPWNY HEPQMGTYDF VGGKDLEYFL QLANDTGLLV ILRAGPYICA
EWDMGGLPAW LLEKKSIVLR SSDSDYLDAV ERWMGVLLPK MRPYLYQNGG PIIMVQVENE
YGSYFACDYN YLRFLLKLFR LHLGDEVVLF TTDGASQFHL KCGALQGLYA TVDFAPGGNV
TAAFLAQRSS EPKGPLVNSE FYTGWLDHWG HRHSVVPAQT IAKTLNEILA CGANVNLYMF
IGGTNFAYWN GANMPYMPQP TSYDYDAPLS EAGDLTEKYF ALRKVIGMYK QLPEGLIPPT
TPKFAYGKVR LQKAGTVLEV LDGLSRSGPV RSTYPLTFVE LKQYFGYVLY RTTLPKNCVE
PTPLSSPLNG VHDRAYVSVD GITKATLIIF NHMRKIRKHI VDAYQMVPQG VLERDKSLEI
NITGQAGANL DILVENMGRV NFGRYNNDFK GLVSNLTLAQ DVLVGWEIYP LDIDGAVNYD
IIYLLHHPKR PAFKELSYEV PTFYTGTLSI PGGIPDLPQD TYVNFPGWTK GQIWINGFNL
GRYWPARGPQ LTLYVPRDVL VASVPNNITV LELERSPCST QACDIEFVDE PNINATLQHE
TDKPPLFVRE LWMGHL
//
