ID   A0A345HX96_9ACTN        Unreviewed;       448 AA.
AC   A0A345HX96;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:AXG81320.1};
GN   ORFNames=DVK44_30535 {ECO:0000313|EMBL:AXG81320.1};
OS   Streptomyces paludis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2282738 {ECO:0000313|EMBL:AXG81320.1, ECO:0000313|Proteomes:UP000253868};
RN   [1] {ECO:0000313|Proteomes:UP000253868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSSD-12 {ECO:0000313|Proteomes:UP000253868};
RA   Zhao J.;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU361152};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC       {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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DR   EMBL; CP031194; AXG81320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345HX96; -.
DR   KEGG; spad:DVK44_30535; -.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000253868; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05297; GH4_alpha_glucosidase_galactosidase; 1.
DR   Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW   Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253868}.
FT   DOMAIN          209..414
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         183
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         213
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            123
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   448 AA;  48944 MW;  BA6856DB0ABB33F0 CRC64;
     MTRIAPATRT LRTAPVKIAF IGAGSVVFTQ GLLADLFAFP ELHGLHVALH DIDPERLDTA
     LGAARRIAQQ TGAAPHITVH AERRAALEGA DFVINIVQVG MGASTRTDFE VPARYGLRQT
     IGDTLGIGGI FRALRTFPLL ASLGADIAAV CPDAWLLNYT NPMAMNVQYL TRATGLTRVV
     GLCHSVYWTM RDLSALLNVP YEEVTYRAAG VNHQAWVLRF EHNGTDLYPR LDALVADDPQ
     LRRRVRVDMY RRLGYYPTET SEHSAEYVPW YLHHDSEIER LRLPVGAYLG IVDENVAAYE
     KTRDALAAGT PLTVESTMEY APQIVHSITT GTPRTVYGNV PNHGLIDNLP ATGTVEVPCL
     VDALGVQPTR IGALPAQCAA LNRSYLSMNE LVVRAALEDD PRSVRQAAMA DPATAAALPV
     ERIWELCDDM VRAHGELLQP SLRATLGS
//