ID   PGGHG_DICDI             Reviewed;         713 AA.
AC   Q54KX5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 90.
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};
DE   Flags: Precursor;
GN   Name=pgghg {ECO:0000250|UniProtKB:Q32M88};
GN   Synonyms=athl1 {ECO:0000312|dictyBase:DDB_G0287109}; ORFNames=DDB_G0287109;
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: 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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR   EMBL; AAFI02000096; EAL63919.2; -; Genomic_DNA.
DR   RefSeq; XP_637395.2; XM_632303.2.
DR   AlphaFoldDB; Q54KX5; -.
DR   SMR; Q54KX5; -.
DR   STRING; 44689.DDB0266682; -.
DR   PaxDb; Q54KX5; -.
DR   EnsemblProtists; EAL63919; EAL63919; DDB_G0287109.
DR   GeneID; 8625926; -.
DR   KEGG; ddi:DDB_G0287109; -.
DR   dictyBase; DDB_G0287109; athl1.
DR   eggNOG; KOG4125; Eukaryota.
DR   HOGENOM; CLU_006285_4_2_1; -.
DR   InParanoid; Q54KX5; -.
DR   OMA; ATHRIYA; -.
DR   PhylomeDB; Q54KX5; -.
DR   PRO; PR:Q54KX5; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0047402; F:protein-glucosylgalactosylhydroxylysine glucosidase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..713
FT                   /note="Protein-glucosylgalactosylhydroxylysine glucosidase"
FT                   /id="PRO_0000330917"
FT   ACT_SITE        451
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q32M88"
FT   BINDING         317..318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         521..522
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        535
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        576
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        662
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   713 AA;  80522 MW;  9513847136611EFF CRC64;
     MIINSQEYLQ PPQWWNERVE AGNLLSISNG EQEPTNYLMT NVGNGYVAFV IGGESIYVGG
     VYNGPAINLG DANNLPSHRA GIPNFQNIEI SNAQFQYAGL DIENATYTRV YSIPSSPGTI
     VKQIFYAHQK IRNILVQEIE VDNSNIETDV TLQLSVVGIN LTANVDFNIL NLTNTQFTGN
     DYQLYNLTIK VPEVNFMTSV AVTTTTIPQS ITIKSGEKKK HHYVTSFLTN IETNDYIEGS
     LDIYKTTFLL ADQLIKSHLD EWNKIWISGI EVGGDSHLQQ VVNSSLYYLF SSIRDDWSYG
     MSPGGLASDG YNGHSFWDTE TWMLPPILLL NPKLVRDCLL QYRINNLPGA HEKALSYKSN
     NYTGFMFPWE SAFTGIEVCP TFAPTGILEQ HITADIALAI RQYYYLTGDL DWLIDFGYKA
     LKGIAEFWAS RVEYDQLNQQ YSINTIIPPD EYAVGVNNSV YTNVAVKMTF EWVIEVATLI
     NDTENIPFEH WSSIANGLVI LFDEVNQWHP EYQGYNGETI KQADVVLLGF PLMYNMSKEA
     RKNDLIYYEA VTTNSGPAMT YSMHTVAWLE LESLENATKQ WFRSYNNCNN SPFLVWTETP
     TGGAVNFATG MGGFLQGLMF GYGGVRIHQG NLDFYPQLPE GTTSLKIRSM NYIGSTFNVG
     WNQTTITFEM LTFNPSVYLT LLSTEYDNII LNTLDPIYLT FGSKFQIYFN NNN