ID   PGGHG_DANRE             Reviewed;         655 AA.
AC   A0JMP0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Protein-glucosylgalactosylhydroxylysine glucosidase {ECO:0000250|UniProtKB:Q32M88};
DE            EC=3.2.1.107 {ECO:0000250|UniProtKB:Q32M88};
DE   AltName: Full=Acid trehalase-like protein 1 {ECO:0000250|UniProtKB:Q32M88};
GN   Name=pgghg {ECO:0000250|UniProtKB:Q32M88};
GN   Synonyms=athl1 {ECO:0000250|UniProtKB:Q32M88}; ORFNames=zgc:154078;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of glucose from the disaccharide
CC       unit linked to hydroxylysine residues of collagen and collagen-like
CC       proteins. {ECO:0000250|UniProtKB:Q32M88}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-
CC         hydroxy-L-lysyl-[collagen] + H2O = (5R)-5-O-(beta-D-galactosyl)-5-
CC         hydroxy-L-lysyl-[collagen] + D-glucose; Xref=Rhea:RHEA:11068,
CC         Rhea:RHEA-COMP:12753, Rhea:RHEA-COMP:12754, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:133443, ChEBI:CHEBI:133452;
CC         EC=3.2.1.107; Evidence={ECO:0000250|UniProtKB:Q32M88};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR   EMBL; BC125951; AAI25952.1; -; mRNA.
DR   RefSeq; NP_001071193.1; NM_001077725.1.
DR   AlphaFoldDB; A0JMP0; -.
DR   SMR; A0JMP0; -.
DR   STRING; 7955.ENSDARP00000004006; -.
DR   CAZy; GH65; Glycoside Hydrolase Family 65.
DR   PaxDb; A0JMP0; -.
DR   PeptideAtlas; A0JMP0; -.
DR   GeneID; 777617; -.
DR   KEGG; dre:777617; -.
DR   CTD; 80162; -.
DR   ZFIN; ZDB-GENE-061103-319; pgghg.
DR   eggNOG; KOG4125; Eukaryota.
DR   InParanoid; A0JMP0; -.
DR   OrthoDB; 125022at2759; -.
DR   PhylomeDB; A0JMP0; -.
DR   PRO; PR:A0JMP0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0047402; F:protein-glucosylgalactosylhydroxylysine glucosidase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..655
FT                   /note="Protein-glucosylgalactosylhydroxylysine glucosidase"
FT                   /id="PRO_0000329006"
FT   ACT_SITE        388
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q32M88"
FT   BINDING         258..259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         456..457
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ   SEQUENCE   655 AA;  72439 MW;  B549B3F4F60FC897 CRC64;
     MGGVYNGDGG TCHRGNIPCP LAAQMKTGEV GRQLYELNMH TGVFSHTVVT SDFEAIQVLY
     AHRNQSNLLV MEILLKRIKT SAEPITIQLE SSFKPQSEDI AFQNAPDYKG GRHIFGQTAS
     SEVPGGVRPV VHLIWTPVTP TLTLPANQSQ SSWTFLVAVA RSNESAQSFY DSGLALINTG
     DLRPSHQRSW AELWKGSSIE VIGAESLNRA LIGCMFYLLG SFPYVNKEAS AAFEFGGVSP
     GGLSNGSEDE DYHGHVFWDQ DTWMYPSIAL FYPALARAVL QYRVETLEGA QVNAQQMGCK
     GLKFAWESAV TGVDVCPEDV YSQQELHING DVILAFQQYY YLTQDLELFQ SGRGSEVVWG
     VADFWVSRVT WDSADQQYHI KGVIPPDEYY FTVDNSVFTN AVAQRSLEFA VELSALLAEV
     PPPAWQDIAD KIKIPFDPEL KFHPEFDGYK PGNKVKQADV VLLGFPLAFP MSPEIRRNDL
     EMYEAVTDPL GPAMTWGMFA LGWLELGEAE KAQKLLQKCF KNVQKPFQVW SESADGSGCV
     NFLTGMGGFL QAVLFGYTGF RVQKEQLAFS PLLPLDVSAL SVKGVCYLGH KMDWTITSEE
     VKVSVRKTDS KETFTLQVVL NSGSTLLLTP GQSVSFPRQP GHICQLKSSS SCWPI