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Database: UniProt
Entry: A0A1Y5KPD3_9BACL
LinkDB: A0A1Y5KPD3_9BACL
Original site: A0A1Y5KPD3_9BACL 
ID   A0A1Y5KPD3_9BACL        Unreviewed;       506 AA.
AC   A0A1Y5KPD3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:OUS77807.1};
GN   ORFNames=B1748_03230 {ECO:0000313|EMBL:OUS77807.1};
OS   Paenibacillus sp. MY03.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS77807.1, ECO:0000313|Proteomes:UP000195591};
RN   [1] {ECO:0000313|EMBL:OUS77807.1, ECO:0000313|Proteomes:UP000195591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MY03 {ECO:0000313|EMBL:OUS77807.1,
RC   ECO:0000313|Proteomes:UP000195591};
RA   Liu H., Cheng Y., Gu J.Y., Han W.J.;
RT   "Draft genome of a polysaccharide-degrading bacterium Paenibacillus sp.
RT   MY03.";
RL   Submitted (MAR-2017) 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:OUS77807.1}.
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DR   EMBL; MXQD01000004; OUS77807.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5KPD3; -.
DR   OrthoDB; 9808275at2; -.
DR   Proteomes; UP000195591; 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   Reference proteome {ECO:0000313|Proteomes:UP000195591}.
FT   DOMAIN          196..414
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   REGION          474..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         150
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   506 AA;  56430 MW;  C0718FDF533DDC56 CRC64;
     MSSYKITFIG AGSIGFTRGL LRDLLSVPEF ANTEVAFTDI NEHNLRMVTE LCQRDIDENG
     LSIRIQATTD RRSALQGAKY VICTIRAGGL EAFATDIDIP LKYGVDQCVG DTLSAGGIMY
     GQRGIAAMLD ICRDIRECAS EDVLLLNYAN PMAMLTWACN KYGGVRTIGL CHGVQGGHWQ
     IATAFGLEKK EVDIICAGIN HQTWYISIKH RGEDLTGRLL EAFENHEDFS RTEKVRIDML
     RRFGYYSTES NGHLSEYVPW YRKRPEEIGD WIDLGSWING ETGGYLRVST EGRNWFETDF
     PNWMKEPAYE YKGEKRGEEH GSYIIESLET GRVYRGHFNV VNNGVISNLP DDAIIEAPGY
     VDRNGISMPH VGELPLGPAA VCNVSISVQR LAVEAAVSGD DQLLRQAFMM DPLVGAVCNP
     KEIWQMVDEM LVAGEQWLPQ YGDAIDAARE RLEKGPLLPT RDYKGAARLK IKTVEEMQQD
     RESANRNAGE SDKGKDREKT ATSSNG
//
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