ID A0A3N2R7L7_9RHOB Unreviewed; 453 AA.
AC A0A3N2R7L7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:ROU03480.1};
GN ORFNames=EAT49_04065 {ECO:0000313|EMBL:ROU03480.1};
OS Histidinibacterium lentulum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Histidinibacterium.
OX NCBI_TaxID=2480588 {ECO:0000313|EMBL:ROU03480.1, ECO:0000313|Proteomes:UP000268016};
RN [1] {ECO:0000313|EMBL:ROU03480.1, ECO:0000313|Proteomes:UP000268016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B17 {ECO:0000313|EMBL:ROU03480.1,
RC ECO:0000313|Proteomes:UP000268016};
RA Wang G.;
RT "Histidinibacterium lentulum gen. nov., sp. nov., a marine bacterium from
RT the culture broth of Picochlorum sp. 122.";
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:ROU03480.1}.
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DR EMBL; RDRB01000002; ROU03480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2R7L7; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000268016; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000268016}.
FT DOMAIN 196..417
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 110
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 453 AA; 50846 MW; C4649555C05AC9BA CRC64;
MTTITFIGAG STVFTKNIAG DVLQRPSLAG ATIRLMDINP KRLEESEIVV AKLIQTLDVP
ATVETYTDRR RALDGADFVV VCFQIGGYDP CTITDFEVPK KFGLRQTIAD TLGIGGIMRG
LRTVPVLWDL CADMTEVCPD AIMLQYVNPM AINTWAIGAK YPAIRQVGLC HSVQGTASEL
ARDLDIPVSE IRYRVGGINH MAFFLQFEHR QPDGSYRDLY PALQQGYAEG RFPKPSSWNP
RCPNKVRYEM LKRLGYFVTE SSEHFAEYTP WFIKRDRPDL IEKFGIPLDE YPKRCVEQIA
RWEKQAKEYR EANEITVAPS DEYASQIMHS VVTGEPGVIY GNIPNRGYIP QLPEGSAVEV
PTLVDASGLQ PTVVRDIPPQ LIGLIRTNLN VQELTVAALV QENREHIYHA AMLDPHTAAE
LDLEQIWALV DDLLVAHDDW LPEFARMGVR RAS
//
