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Database: UniProt
Entry: A0A1S1QF78_9ACTN
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Original site: A0A1S1QF78_9ACTN 
ID   A0A1S1QF78_9ACTN        Unreviewed;       441 AA.
AC   A0A1S1QF78;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:OHV31905.1};
GN   ORFNames=BCD49_06520 {ECO:0000313|EMBL:OHV31905.1};
OS   Pseudofrankia sp. EUN1h.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Pseudofrankia.
OX   NCBI_TaxID=1834515 {ECO:0000313|EMBL:OHV31905.1, ECO:0000313|Proteomes:UP000179465};
RN   [1] {ECO:0000313|Proteomes:UP000179465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EUN1h {ECO:0000313|Proteomes:UP000179465};
RA   Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA   Nouioui I., Abebe-Akele F., Thomas K., Gtari M., Tisa L.S.;
RT   "Sequence Frankia sp. strain EUN1h.";
RL   Submitted (JUL-2016) 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}.
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:OHV31905.1}.
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DR   EMBL; MBLN01000077; OHV31905.1; -; Genomic_DNA.
DR   RefSeq; WP_007510067.1; NZ_MBLN01000077.1.
DR   AlphaFoldDB; A0A1S1QF78; -.
DR   Proteomes; UP000179465; Unassembled WGS sequence.
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   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}.
FT   DOMAIN          197..403
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         171
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         201
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            111
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   441 AA;  48470 MW;  D5F3C094CD4F084C CRC64;
     MTTVCFVGAG SAEFTRQLLR DLLTYDDLGP LTLVMHDVDP RRLELAENLA RIAVERHGRD
     ATTTIRGSLD RAAALHGADF VINAVNIGGH AATLTDFEVP ARFGLRQTIA DTLGPGGVFR
     GLRTFGFLDD LATDLRAEAP DAWLLNYTNP MAMNIQFLSV RHPELKVLGL CHSVYWTVHD
     LCELIDVPFD DVSFHSAGVN HQAWVLRFER DGVDLYPELD RRIAADPQLR RRVRVDMYRR
     LGFYPTETSE HSAEYVPWYL REPGEIERLR IPIDDYVGIS ARNLADVEAL MPVVAAGGYV
     EPEEEAAEYA PQVIHSMVTG TARTIQATVR NDALIDNLPD GAAVEVPCRV DANGAAPLPV
     GDLPAQCAAL NRTFLSVVDL TVRAATLGRP DHIRHALMAD PNTAASLSVE EIWRLADELV
     AAHGERLPQP LRARLGDPGG S
//
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