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Database: UniProt
Entry: A0A494Y7T7_9BURK
LinkDB: A0A494Y7T7_9BURK
Original site: A0A494Y7T7_9BURK 
ID   A0A494Y7T7_9BURK        Unreviewed;       478 AA.
AC   A0A494Y7T7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:RKP58426.1};
GN   ORFNames=D7S86_00190 {ECO:0000313|EMBL:RKP58426.1};
OS   Pararobbsia silviterrae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Pararobbsia.
OX   NCBI_TaxID=1792498 {ECO:0000313|EMBL:RKP58426.1, ECO:0000313|Proteomes:UP000270342};
RN   [1] {ECO:0000313|EMBL:RKP58426.1, ECO:0000313|Proteomes:UP000270342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DHC34 {ECO:0000313|EMBL:RKP58426.1,
RC   ECO:0000313|Proteomes:UP000270342};
RA   Gao Z.-H., Qiu L.-H.;
RT   "Robbsia sp. DHC34, isolated from soil.";
RL   Submitted (OCT-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}.
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:RKP58426.1}.
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DR   EMBL; RBZU01000001; RKP58426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494Y7T7; -.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000270342; 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   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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000270342}.
FT   DOMAIN          199..440
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         174
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         204
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            115
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   478 AA;  53253 MW;  9A8FFA3448C9C1A4 CRC64;
     MASKRPIKIT LVGAGSTVFA RNLLGDILAY PELADSEIAL YDIDEKRLGL SELVAQRVAG
     HLGVKPRIVA TTDRARALDG ADYALNMIQV GGYKPSTVID FEIPKRYGLE QTIGDTLGIG
     GIMRGLRTIP VMLDILGDME RLCPDVVHLN YVNPMAILCW AISRASRIRT VGLCHSVQGT
     AAELAEDIGV PFEEIDYLCA GINHMAFYLK FERAGRDLYP ELHRVRAEGR VPDFNRVRYE
     MLHRLGYFPT ESSEHFSEYV PWFIKRGREE LLEKFNIPLD EYPGRCQVYE ASWEYFEKEL
     REPGSQDPEA LRAALLASGI KVMDKRHDGA VRNLEGLRKV RRSVEYGATI IHAIETGSPK
     VIYGNVPNHR LIDNLPEGCC VEVPCLVDAN GVQPTRIGAL PPQLAALMRT NIGVQELTVE
     AALTGRRDHV YHAAMLDPHT AAELDVEQIV SLVDDLLDAH RDRLPESLQR GSRVELAA
//
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