BGAL1_DICDI
ID BGAL1_DICDI Reviewed; 671 AA.
AC Q54GE1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Beta-galactosidase 1;
DE EC=3.2.1.23;
DE AltName: Full=Acid beta-galactosidase 1;
DE Short=Lactase 1;
DE Flags: Precursor;
GN Name=glb1; ORFNames=DDB_G0290217;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; AAFI02000161; EAL62330.1; -; Genomic_DNA.
DR RefSeq; XP_635837.1; XM_630745.1.
DR AlphaFoldDB; Q54GE1; -.
DR SMR; Q54GE1; -.
DR STRING; 44689.DDB0266380; -.
DR PaxDb; Q54GE1; -.
DR EnsemblProtists; EAL62330; EAL62330; DDB_G0290217.
DR GeneID; 8627545; -.
DR KEGG; ddi:DDB_G0290217; -.
DR dictyBase; DDB_G0290217; glb1.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_7_2_1; -.
DR InParanoid; Q54GE1; -.
DR OMA; RAHPDTW; -.
DR PhylomeDB; Q54GE1; -.
DR Reactome; R-DDI-1660662; Glycosphingolipid metabolism.
DR Reactome; R-DDI-2022857; Keratan sulfate degradation.
DR Reactome; R-DDI-2024096; HS-GAG degradation.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54GE1; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
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 InterPro; IPR026283; B-gal_1-like.
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; 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 3: Inferred from homology;
KW Glycoprotein; Glycosidase; Hydrolase; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..671
FT /note="Beta-galactosidase 1"
FT /id="PRO_0000328062"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 288
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 671 AA; 74979 MW; 27F7DD24EDA31925 CRC64;
MKLIVLIFFL LFINLNYCLK IKEQPKVGGI DSEQPTNSFY IENGNFLMNN QGNGGSLNQY
QIISGSFHYF RCLPELWVDR LTKMKACGLN TIQTYIPWNV HQPNGFNTEL VATNDLIEFL
RQAQQIGLNV ILRPGPYSCA EWELGGFPYW ILEQQPIALR SSDSVFISAV IAYWSRLLPL
LEPLLFTNGG PIIMVQVENE YGSYGEDKSY LETLLTLLQK YLGQGDGNGS GVLFHSTDGP
SAQMLFGSKL EGVYQTVDFG PMPIEQIQDN FKIQQTFASK PTPPMNSEYY TGWITNWGDA
SAARTDASVV AQGLDDILSL NASVNMYMFF GGSNAGFMNG ANSNSPTTNF EITIQSYDYD
SPLSESGDTT EKYFAIKNVI EKYIKPTTNS NSTLPPIPSN STKVAYGTIQ ITQATSLFNN
LANLVNSNQQ QLQTGAPIPM EQLQQSTGFV LYETTMNIAQ SSQLSITELH DRATIFINDE
AIEDTQTIGQ AVFLQRPFNS SIEITYPSNV TDDGNFNLRI LLENQGRVNF GPYLNDRKGL
LSGGVLSGQQ YLGPWNNYPL PLTNKTLSNI NNWEQIKDYT LSNTPTFYQA TLSLNSTNDI
GDTFLSFTGL GKGQLFVNGY NVGRYWNVGP QRTIYISSVL LHQGDNEIIL FETLLTQPIF
EIQFLNQPYF D
