ID A0A172TF36_9BACL Unreviewed; 501 AA.
AC A0A172TF36;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Alpha-galactosidase {ECO:0000313|EMBL:ANE45514.1};
GN ORFNames=SY83_03385 {ECO:0000313|EMBL:ANE45514.1};
OS Paenibacillus swuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE45514.1, ECO:0000313|Proteomes:UP000076927};
RN [1] {ECO:0000313|EMBL:ANE45514.1, ECO:0000313|Proteomes:UP000076927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6 {ECO:0000313|EMBL:ANE45514.1,
RC ECO:0000313|Proteomes:UP000076927};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL Submitted (JAN-2015) 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; CP011388; ANE45514.1; -; Genomic_DNA.
DR RefSeq; WP_068604258.1; NZ_CP011388.1.
DR AlphaFoldDB; A0A172TF36; -.
DR STRING; 1178515.SY83_03385; -.
DR KEGG; pswu:SY83_03385; -.
DR PATRIC; fig|1178515.4.peg.667; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000076927; 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; 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:UP000076927}.
FT DOMAIN 195..413
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT REGION 476..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
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 501 AA; 55955 MW; D98636A50B671ACB CRC64;
MSFKVAFVGA GSIGFTRGLL RDLLSVPEFQ DIQVAFNDIN EHNLDMVTQL CQRDIRENGL
GIEIEASTDR RAVLKDARYV FVVVRIGGLE AFSTDVDIPL KYGIDQCVGD TLCAGGIMYG
QRGIAEMMNI CKDIREVAEP NALMLNYANP MAMLTWACNK YGGVRTIGLC HGVQGGHRQI
ATALGLEKSE VDIICAGINH QTWYVQVQHN GEDMTGKLLE AFENHPEYRQ TEKVRIDMLR
RFGYYSTESN GHLSEYVPWY RKRPEEIMDW IDMGSWINGE TGGYLRVCTE GRNWFETDFP
NWMKEDAVRY RPENRGEEHG SYIIEGLETG RVYLGHFNVV NNGIISNLPD DAIIEAPGYV
DRNGISMPTV GDLPLGCAAV CNVSISVQRM AVEAAIHGDD QLLRQAMMMD PLVGAVCNPK
EIWQMVDEML VAQEAWLPQY SEAIAAAKAR LAEGPLLPTR NYEGAARLKV KSVEEMQQNR
EEANKNAGES DKALERPAAV N
//
