ID W5M551_LEPOC Unreviewed; 644 AA.
AC W5M551;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN Name=GLB1L2 {ECO:0000313|Ensembl:ENSLOCP00000003509.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000003509.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000003509.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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|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 EMBL; AHAT01024150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01024151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M551; -.
DR STRING; 7918.ENSLOCP00000003509; -.
DR Ensembl; ENSLOCT00000003516.1; ENSLOCP00000003509.1; ENSLOCG00000002950.1.
DR eggNOG; KOG0496; Eukaryota.
DR GeneTree; ENSGT00950000182942; -.
DR InParanoid; W5M551; -.
DR OMA; GSEIVHN; -.
DR Proteomes; UP000018468; Linkage group LG26.
DR Bgee; ENSLOCG00000002950; Expressed in brain and 12 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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:SF199; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..373
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 431..532
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 556..615
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 644 AA; 73577 MW; 80C7CDD634BAD4B2 CRC64;
MIILSIRNAQ RRRIAAIGLI LVGVITYYYI RLSAGGNMSS ISRTVMMKIS RKVGLEAESS
EFTLGGEKFR ILGGSVHYFR VPRAYWRDRM KKMKACGLNT LTTYVPWNLH EPERGRFDFK
DQLDLEAFIN LAADVGLWVI LRPGPYICSE WDLGGLPSWL LRDKDMRLRT TYEGFTEAVD
AYFDRLIPIV APLQFKKGGP IIAFQVENEY GSYAMDEEYM PYMKKSLLSR EIDELLMTSD
NKEGFNQGGV EGALATINLQ KLKPEHLNLL EATQPQKPKM VMEYWTGWFD SWGDLHHVFP
TEDMAATVTE ILKKHMSINL YMFHGGTNFG FMSGALEFGT YKPDVVSYDY DAPLSEAGDY
TEKYHLLRNI FSQYHTEKLP LVPALSRKAV YETSIMYHYI SMWEALQFTE EPFKSERPVN
MENLPVNNGN GQSYGYTLYE TTITSGGTLH SNNSVRDRAL VFVDQHFIGI LKSKTLELAV
PEGKGDRKLS LLVENCGRVN YGKHLDDQRK GLVGDILLNN IPLKKFFIYS LDMKPSFIDR
LSGKNWKLVP EKPTFPGFFQ GRLFVDGYPR DTFVKLPGWT KGVVFINGQN LGRYWSIGPQ
QTLYLPGPWL NSGMNQIIVF EEQEAERKIQ LVDTPDLGMA VDIE
//
