GenomeNet

Database: UniProt
Entry: BGAL_PONAB
LinkDB: BGAL_PONAB
Original site: 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   23-MAY-2018, entry version 66.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {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.
CC       {ECO:0000305}.
DR   EMBL; CR860068; CAH92216.1; -; mRNA.
DR   RefSeq; NP_001126295.1; NM_001132823.1.
DR   UniGene; Pab.11639; -.
DR   ProteinModelPortal; Q5R7P4; -.
DR   SMR; Q5R7P4; -.
DR   STRING; 9601.ENSPPYP00000015702; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PRIDE; Q5R7P4; -.
DR   GeneID; 100173272; -.
DR   KEGG; pon:100173272; -.
DR   CTD; 2720; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   HOVERGEN; HBG004841; -.
DR   InParanoid; Q5R7P4; -.
DR   KO; K12309; -.
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   Gene3D; 2.60.120.260; -; 3.
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; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Lysosome; Reference proteome; Signal; Zymogen.
FT   SIGNAL        1     23       {ECO:0000250}.
FT   PROPEP       24     28       {ECO:0000250}.
FT                                /FTId=PRO_0000283037.
FT   CHAIN        29    677       Beta-galactosidase.
FT                                /FTId=PRO_0000283038.
FT   ACT_SITE    188    188       Proton donor.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   ACT_SITE    268    268       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING      83     83       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     129    129       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     187    187       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     333    333       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   CARBOHYD     26     26       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    247    247       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    464    464       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    498    498       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    545    545       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    555    555       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    195    230       {ECO:0000250|UniProtKB:P16278}.
FT   DISULFID    626    634       {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
//
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