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Database: UniProt
Entry: A0A248YND9_9ACTN
LinkDB: A0A248YND9_9ACTN
Original site: A0A248YND9_9ACTN 
ID   A0A248YND9_9ACTN        Unreviewed;       557 AA.
AC   A0A248YND9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Alpha-galactosidase {ECO:0000256|RuleBase:RU361168};
DE            EC=3.2.1.22 {ECO:0000256|RuleBase:RU361168};
DE   AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN   ORFNames=CIK06_15130 {ECO:0000313|EMBL:ASW55223.1};
OS   Plantactinospora sp. KBS50.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Plantactinospora.
OX   NCBI_TaxID=2024580 {ECO:0000313|EMBL:ASW55223.1, ECO:0000313|Proteomes:UP000216795};
RN   [1] {ECO:0000313|EMBL:ASW55223.1, ECO:0000313|Proteomes:UP000216795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS50 {ECO:0000313|EMBL:ASW55223.1,
RC   ECO:0000313|Proteomes:UP000216795};
RA   Juboi H., Hwang S.S., Yeo T.C., Nissom P.M.;
RT   "Genome sequencing and analysis of secondary metabolite biosynthetic
RT   capabilities of Plantactinospora sp. KBS50.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|RuleBase:RU361168};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC       {ECO:0000256|ARBA:ARBA00009743, ECO:0000256|RuleBase:RU361168}.
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DR   EMBL; CP022961; ASW55223.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A248YND9; -.
DR   KEGG; plk:CIK06_15130; -.
DR   OrthoDB; 9807519at2; -.
DR   Proteomes; UP000216795; Chromosome.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd14792; GH27; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002241; Glyco_hydro_27.
DR   InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR041233; Melibiase_C.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR   Pfam; PF16499; Melibiase_2; 1.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361168};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361168};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216795};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..557
FT                   /note="Alpha-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012445055"
FT   DOMAIN          427..555
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   557 AA;  58993 MW;  69FFA562CDCBABA8 CRC64;
     MRRPTGRRRW MAALAAGLLT TGAAVGLHAT AGQALNNGVA RTPPMGWNSW NTFGCNISES
     LIRGMADAIV SSGMRDLGYQ YVVVDDCWFN PNRDSSGNLQ GDPTRFPSGM KALGDYLHGK
     GLKFGIYQVP VDKTCAQYFG AYPGATGSQG HETQDARQFA AWGVDYLKYD WCSPNGTIND
     QITTFARMRD ALAATGRPIV YSINPNSIHS KTGPQRNWGD VANMWRTTED ITNAWDTGQT
     NGYPMGIQNI VNVNVPLASY AGPGQFNDPD MMEIGRGGMT DTEMRSHFAL WAVMASPLIA
     GNDIRSMDSA TQTILKNSRL IAINQDSLAR QAVQVSNDGT RRVLAKPLAN GDVAVALFNQ
     GSSTTTISTT AAAVGKSGSS FTLVDAWSGA SSSSTGSISA SVPGHGTVVY RVSGGGTTTP
     PTTTPPSGAQ KIVGGQSGRC VDVPNSSTTN GTQVQLYDCW STSGQSWTYT SGKQLQVFGN
     KCLDAYNQGT SNGTQVIIWD CNGQSNQQWN VNSNGTITGV QSGLCLDANG AATANGTKII
     LWSCSGAANQ QWSLRAS
//
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