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Database: UniProt
Entry: A0A1F5C0S6_9BACT
LinkDB: A0A1F5C0S6_9BACT
Original site: A0A1F5C0S6_9BACT 
ID   A0A1F5C0S6_9BACT        Unreviewed;       369 AA.
AC   A0A1F5C0S6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:OGD36453.1};
DE   Flags: Fragment;
GN   ORFNames=A2V94_05235 {ECO:0000313|EMBL:OGD36453.1};
OS   Candidatus Atribacteria bacterium RBG_16_35_8.
OC   Bacteria; Atribacterota.
OX   NCBI_TaxID=1797290 {ECO:0000313|EMBL:OGD36453.1, ECO:0000313|Proteomes:UP000176442};
RN   [1] {ECO:0000313|EMBL:OGD36453.1, ECO:0000313|Proteomes:UP000176442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGD36453.1}.
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DR   EMBL; MEYG01000047; OGD36453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5C0S6; -.
DR   Proteomes; UP000176442; 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; IPR019802; GlycHydrolase_4_CS.
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:SF4; ALPHA-GLUCOSIDASE; 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.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 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|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3}.
FT   DOMAIN          198..369
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
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         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            113
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
FT   NON_TER         369
FT                   /evidence="ECO:0000313|EMBL:OGD36453.1"
SQ   SEQUENCE   369 AA;  41516 MW;  D93C2F310CB98BF7 CRC64;
     MSGIKLSIIG AGSAIFSLKL VGDLCKTKGS SGSSVSLMDI DEKRLNSVHL LAARYAAALG
     ANLKFEKTTD MKRSIEGADF VINTALIGGH GQLDASRKAG EMHGYARGID SQEFNMVSDY
     NTLSNYNQLK YFLEVAHNME EICPNAWLLQ SANPVFEGTT LISRYSDIKV IGFCHGHYGV
     EIVARSLGLD IREVNWQVAG FNHNIWLTRF LYKDKDAYPL LDQWIEKEAM KWKPEDPFDD
     QMSPAAIDMY KFYGRMPIGD SIRNGSWKYH YHLEAKKKWY GEPWGGADSD LGWAWYQNYL
     KASTDKSFKL ALDKSINLLQ EFPPEVMSRE QHIPFIDALI NGNQGRFVLN IPNKGPIIPS
     IPEDVAVEV
//
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