ID   AGAL_STRBB              Reviewed;         635 AA.
AC   D7CFN7;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Probable retaining alpha-galactosidase;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase;
DE   Flags: Precursor;
GN   OrderedLocusNames=SBI_01652;
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=749414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1;
RX   PubMed=20581206; DOI=10.1128/jb.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC         residues in alpha-D-galactosides, including galactose
CC         oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 97 family. {ECO:0000305}.
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DR   EMBL; CP002047; ADI04773.1; -; Genomic_DNA.
DR   RefSeq; WP_014174252.1; NC_016582.1.
DR   AlphaFoldDB; D7CFN7; -.
DR   SMR; D7CFN7; -.
DR   STRING; 749414.SBI_01652; -.
DR   CAZy; GH97; Glycoside Hydrolase Family 97.
DR   PRIDE; D7CFN7; -.
DR   EnsemblBacteria; ADI04773; ADI04773; SBI_01652.
DR   KEGG; sbh:SBI_01652; -.
DR   PATRIC; fig|749414.3.peg.1705; -.
DR   eggNOG; COG1082; Bacteria.
DR   HOGENOM; CLU_011166_1_1_11; -.
DR   OMA; INTHEPI; -.
DR   OrthoDB; 469334at2; -.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR029483; GH97_C.
DR   InterPro; IPR019563; GH97_catalytic.
DR   InterPro; IPR029486; GH97_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF14509; GH97_C; 1.
DR   Pfam; PF14508; GH97_N; 1.
DR   Pfam; PF10566; Glyco_hydro_97; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW   Reference proteome; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..635
FT                   /note="Probable retaining alpha-galactosidase"
FT                   /id="PRO_0000415273"
FT   ACT_SITE        397
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        452
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         446
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         452
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   635 AA;  69484 MW;  A1FD48A9BC4CCD93 CRC64;
     MARSVRRTTL ALLLSAVLAM TLFVTAPAHA QDSTWTVSGP SARSGPQARL QLDATTGALT
     LQVSRGGRTV LEPSPLGIRT EGADLSRGLR LSGRERRVVA ERYRTAVGKQ RSRDVRMTET
     RFRFRGDGGA RFDLVVRVSD DGVAYRYVLP KGSGDVLGET SAFTLPTDAT AWLGAYRRDN
     ENLFNQYPAA TAPTGEYMAQ ALFETRGTYA LIAESDLSGR YSAARLIHEA GLPTYRIGLW
     DERVTSDGAL STPWRALVVG DLATVTESTF TDDLAPASRV ADTSWIRPGP ALWTWLAGGK
     PAGQSLSMQK GYVDYAAQRG WPYVVVDAGW YFDPDQWDVT DPDWQTNSWI PELVTYARER
     GVGIQVWIHH RDLDTAEERE QWLPTLERWG VKGVKIDFMD SESQDTLRWY DEILPATAAH
     HLLVNFHGST IPKGIQRTWP HVMTMEGVNG EEKRVNTAQH LTTLPFTRNV IGSMDFTPGA
     FHRPQRPNAA SDAGELGLSV LYESGIQNLA GTPESYDARP LARGFLEQLP AAWDRTRLLA
     GRPGESAVLA RASGGRWFIG GTFAGAAHTA EVPLRLGSGT WLVDLVLDGP DGLVREPRVV
     RGGDTLSVPV VADGGFAAIA CHWRPGRTSC DRTAA