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Database: UniProt
Entry: W4AEY3_9BACL
LinkDB: W4AEY3_9BACL
Original site: W4AEY3_9BACL 
ID   W4AEY3_9BACL            Unreviewed;       433 AA.
AC   W4AEY3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Alpha-galactosidase {ECO:0000313|EMBL:ETT29612.1};
GN   ORFNames=C161_28963 {ECO:0000313|EMBL:ETT29612.1};
OS   Paenibacillus sp. FSL R5-192.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT29612.1, ECO:0000313|Proteomes:UP000019041};
RN   [1] {ECO:0000313|EMBL:ETT29612.1, ECO:0000313|Proteomes:UP000019041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT29612.1,
RC   ECO:0000313|Proteomes:UP000019041};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
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:ETT29612.1}.
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DR   EMBL; ASPR01000078; ETT29612.1; -; Genomic_DNA.
DR   RefSeq; WP_036674667.1; NZ_ASPR01000078.1.
DR   AlphaFoldDB; W4AEY3; -.
DR   PATRIC; fig|1226754.4.peg.5824; -.
DR   Proteomes; UP000019041; 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}.
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   433 AA;  48888 MW;  35596B39CCB07522 CRC64;
     MNKITFLGAG STVFVKNVLG DVMMTEALQD FELALFDIDA ERLSDSERLL TSLARSLGSR
     CVVNVYHDRK EALRGAKYVI NAIQVGGYDP CTITDFEIPK KYGLRQTIAD TLGIGGIFRN
     LRTIPVMLDF ARDMQEVCPD AWFLNYTNPM AVLTNVMNVH GGIKTVGLCH SVQVCVPHLF
     DALGIDQTGV VAKIAGINHM AWLLEVTKDG QDLYPEIKRL AKEKQKEQHD DMVRFELMQR
     FGYYVTESSE HNAEYHPYFI KRNYPELIER FNIPLDEYPR RCVNQIEGWK EMRTKLFASE
     NIEHTRSREY ASHIIEAMET NNPYKIGGNV MNNGLITNLP REACVEVPCL VDGSGISPTY
     IGDLPPQLAA LNRTNINTQL LTIEAAITEK KEHIYHAAML DPHTAAELSI DDIVAMCDEL
     IEAHGDWLPK YTS
//
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