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Database: UniProt
Entry: A0A2Z2KEX1_9BACL
LinkDB: A0A2Z2KEX1_9BACL
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ID   A0A2Z2KEX1_9BACL        Unreviewed;       435 AA.
AC   A0A2Z2KEX1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:ASA21700.1};
GN   ORFNames=B9T62_13540 {ECO:0000313|EMBL:ASA21700.1};
OS   Paenibacillus donghaensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=414771 {ECO:0000313|EMBL:ASA21700.1, ECO:0000313|Proteomes:UP000249890};
RN   [1] {ECO:0000313|EMBL:ASA21700.1, ECO:0000313|Proteomes:UP000249890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 13049 {ECO:0000313|EMBL:ASA21700.1,
RC   ECO:0000313|Proteomes:UP000249890};
RA   Jung B.K., Hong S.-J., Shin J.-H.;
RT   "Complete genome sequence of Paenibacillus donghaensis KCTC 13049T isolated
RT   from East Sea sediment, South Korea.";
RL   Submitted (JUN-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}.
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DR   EMBL; CP021780; ASA21700.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z2KEX1; -.
DR   KEGG; pdh:B9T62_13540; -.
DR   OrthoDB; 9808275at2; -.
DR   Proteomes; UP000249890; Chromosome.
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:UP000249890}.
FT   DOMAIN          194..404
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         169
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         199
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   435 AA;  48811 MW;  746FFE371309A935 CRC64;
     MPKITFIGAG STVFAKNVLG DCMQTPALQG FELALFDIDL QRLNDSENML NHIKASSGST
     CQVKSYTDRK EALRGASYVI NAIQVGGYDP STIIDFEIPK KYGLRQTIAD TAGIGGIFRN
     LRTIPVMLDF AAEMREVCPD ALFLNYTNPM AVLTNVMNTY GGVQTVGLCH SVQQCIPGLF
     EHLGIDQTGV QAKIAGINHM AWLLEVTKNG EDLYPEIKRR AAEKQQEHHG DMVRYEMMLK
     FGYYITESSE HNAEYHPYFI KRHYPELIER FQIPLDEYPR RCVEQISNWQ QMREELVGNK
     QLEHTRSHEY ASYILEAMET NIPFKIGGNV MNTGLITNLP REACVEVPCL VDSSGVTPTF
     VGDLPPQCAA LNRTNINTQL LTIEAAMTRK KDHIYHAAML DPHTSAELSM DDIVSMCDEL
     IAAHTATGFL QDVYK
//
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