BGAL_PONAB
ID BGAL_PONAB Reviewed; 677 AA.
AC Q5R7P4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Beta-galactosidase;
DE EC=3.2.1.23 {ECO:0000250|UniProtKB:P16278};
DE AltName: Full=Acid beta-galactosidase;
DE Short=Lactase;
DE Flags: Precursor;
GN Name=GLB1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans.
CC {ECO:0000250|UniProtKB:P16278}.
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:0000250|UniProtKB:P16278};
CC -!- SUBUNIT: Homodimer. May form higher multimers.
CC {ECO:0000250|UniProtKB:P16278}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P16278}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; CR860068; CAH92216.1; -; mRNA.
DR RefSeq; NP_001126295.1; NM_001132823.1.
DR AlphaFoldDB; Q5R7P4; -.
DR SMR; Q5R7P4; -.
DR STRING; 9601.ENSPPYP00000015702; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR GeneID; 100173272; -.
DR KEGG; pon:100173272; -.
DR CTD; 2720; -.
DR eggNOG; KOG0496; Eukaryota.
DR InParanoid; Q5R7P4; -.
DR OrthoDB; 179316at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004565; F:beta-galactosidase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
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; PTHR23421; 1.
DR Pfam; PF13364; BetaGal_dom4_5; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Reference proteome; Signal; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT PROPEP 24..28
FT /evidence="ECO:0000250"
FT /id="PRO_0000283037"
FT CHAIN 29..677
FT /note="Beta-galactosidase"
FT /id="PRO_0000283038"
FT REGION 654..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 195..230
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT DISULFID 626..634
FT /evidence="ECO:0000250|UniProtKB:P16278"
SQ SEQUENCE 677 AA; 75932 MW; F918E217E84BC7B5 CRC64;
MPGFLVRILP LLLALLLLGP TRGLRNATQR MFEIDYSRDC FLKDGQPFRY ISGSIHYSRV
PRFYWKDRLL KMKMAGLNAI QTYVPWNFHE PWPGQYQFSE DHDVEYFLQL AHELGLLVIL
RPGPYICAEW EMGGLPAWLL EKESILLRSS DPDYLAAVDK WLGVLLPKMK PLLYQNGGPV
ITVQVENEYG SYFACDFDYL RFLQKCFRHH LGDDVVLFTT DGAHKTFLKC GALQGLYTTV
DFGTGSNITD AFLSQRKCEP KGPLINSEFY TGWLDHWGQP HSTIKTEAVA SSLYDILARG
ASVNLYMFIG GTNFAYWNGA NTPYAAQPTS YDYDAPLSEA GDLTEKYFAL RNIIQKFEKV
PEGPIPPSTP KFAYGKVALE KLKTVGAALD ILCPSGPIKS LYPLTFIQVK QHYGFVLYRT
TLPQDCSNPA PLSSPFNGVH DRAYVAVDGI PQGVLERNNV ITLNITGKAG ATLDLLVENM
GRVNYGAYIN DFKGLVSNLT LSSNILTDWT IFPLDTEDAV RSHLGGWGHR DSGHHDEAWA
HSSSNYTLPA FYVGNFSIPS GIPDLPQDTF IQFPGWTKGQ VWINGFNLGR YWPARGPQLT
LFVPQHILMT SAPNTITMLE LERAPCSNDD PELCAVTFVD RPVIGSSVTY DHPSKPVEKK
LMPSPPQKNK DSWLDHV
