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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//