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Database: UniProt
Entry: A0A0B2UY78_TOXCA
LinkDB: A0A0B2UY78_TOXCA
Original site: A0A0B2UY78_TOXCA 
ID   A0A0B2UY78_TOXCA        Unreviewed;       689 AA.
AC   A0A0B2UY78;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   Name=GLB1 {ECO:0000313|EMBL:KHN73780.1};
GN   ORFNames=Tcan_18463 {ECO:0000313|EMBL:KHN73780.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN73780.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN73780.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN73780.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KHN73780.1}.
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DR   EMBL; JPKZ01003059; KHN73780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2UY78; -.
DR   STRING; 6265.A0A0B2UY78; -.
DR   OMA; TNKEMIC; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF165; 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:UP000031036};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          65..383
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          434..542
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          575..629
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        213
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        295
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   689 AA;  78771 MW;  8030D07956E6B809 CRC64;
     MKIVHCICPN KLNERIRSEG ICSKILTSSN MQHLPLVLTI LLIFGGALVY SQSVPSFTID
     RDNKQFLLDG KPFRYISGSI HYFRVHPDQW NDRLFRMRAA GLNAIQFYIP WNFHEVYEGK
     PQFEGSRNIT RFLQLAMQNE LYALVRIGPF TCGEWESGGH PWWLLKYKDI KMRTSDERYL
     AAVKRWFDIL LPMLKPSLRK NGGPILMLQL ENEYGSFSGC DRNYTAFLRD LAKSHFGDDV
     VLYTTDGGDD SYLKCGTIPG VFATVDFGPT SREGIEHGFA AQRHYEPNGP LVNSEYYPGW
     FLLWNQKQPS DQPVHNVING SMYMFELGAS FNYYMFHGGT NFAFWNGGFP KTAVTTSYDY
     FAPLSEAADV TDKYIAVRDW IKTIEHWPNP PKTLPKNNPK TAYGVVPMRR ITSLVSNETL
     QVASNGRSLS WRYPLTFEEL QHPFGFVVYR SKLTKSGGNL SIPLFKDYAY VFVGEKYQGM
     LIDSLDDYEK RWLMIKGEIG DDLAIMIENR GRNIGNINDF KGILSNVTID GSIMENWEHF
     PIPLPYLYDE VIGNLSSLIQ RKIKDAKQRT VSGTPGLYAG HFNAKSQDDT FLNPQGWGKG
     QVFVNGFNVG RYWPSVGPQV TLYVPSSIIC KRNMVLIMEL TDASICSQSK CTVEFIDHPI
     FNFTSPTVAS HFRRDDFRMK KLRDNLTSL
//
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