ID W0FTM7_9BACT Unreviewed; 389 AA.
AC W0FTM7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Alpha-galactosidase, NAD(P)-binding {ECO:0000313|EMBL:AHF26924.1};
DE Flags: Fragment;
OS uncultured bacterium Contig1214.
OC Bacteria; environmental samples.
OX NCBI_TaxID=1393399 {ECO:0000313|EMBL:AHF26924.1};
RN [1] {ECO:0000313|EMBL:AHF26924.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24223817;
RA Wang L., Hatem A., Catalyurek U.V., Morrison M., Yu Z.;
RT "Metagenomic insights into the carbohydrate-active enzymes carried by the
RT microorganisms adhering to solid digesta in the rumen of cows.";
RL PLoS ONE 8:E78507-E78507(2013).
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; KC247014; AHF26924.1; -; Genomic_DNA.
DR AlphaFoldDB; W0FTM7; -.
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; 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: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.
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|PIRSR:PIRSR601088-3};
KW NAD {ECO:0000256|RuleBase:RU361152};
KW Nickel {ECO:0000256|PIRSR:PIRSR601088-3}.
FT DOMAIN 136..359
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 111
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 141
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 51
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHF26924.1"
SQ SEQUENCE 389 AA; 43909 MW; 2F2185CC50D7F228 CRC64;
SGKITCHTQQ KEALEDADFV VVAFQIGGYE PCTVTDFEVC KRHGLEQTIA DTLGPGGIMR
ALRTIPHLWQ ICEDMTEVCP DATMLNYVNP MAMNTWAMYA RYPHIKQVGL CHSVQGTAEE
LARDLNIDPA TLRYRCAGIN HMAFYLELER KTADGSYVNL YPELLAAYEA GQAPKPNIHG
NTRCQNIVRY EMFKKLGYFV TESSEHFAEY TPWFIKPGRE DLIERYKVPL DEYPKRCVEQ
LANWHKELEE YKKASRIDIK PSREYASTIM NAIWTGEPSV IYGNVRNDGL IDNLPQGCCV
EVACLVDANG IQPTKVGTLP SHLAALMQTN INVQTLLTEA ILTENRDRVY HAAMMDPHTA
AVLGIDEIYA LVDDLIAAHG DWLPGWLHR
//
