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Database: UniProt
Entry: I0L114_9ACTN
LinkDB: I0L114_9ACTN
Original site: I0L114_9ACTN 
ID   I0L114_9ACTN            Unreviewed;       608 AA.
AC   I0L114;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=MILUP08_42432 {ECO:0000313|EMBL:CCH17511.1};
OS   Micromonospora lupini str. Lupac 08.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH17511.1, ECO:0000313|Proteomes:UP000003448};
RN   [1] {ECO:0000313|Proteomes:UP000003448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX   PubMed=22815450; DOI=10.1128/jb.00628-12;
RA   Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA   Carro L., Coll P., Trujillo M.E.;
RT   "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT   Nodules of Lupinus angustifolius.";
RL   J. Bacteriol. 194:4135-4135(2012).
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}.
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:CCH17511.1}.
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DR   EMBL; CAIE01000018; CCH17511.1; -; Genomic_DNA.
DR   RefSeq; WP_007458227.1; NZ_HF570108.1.
DR   AlphaFoldDB; I0L114; -.
DR   STRING; 1150864.MILUP08_42432; -.
DR   eggNOG; COG3345; Bacteria.
DR   eggNOG; COG3507; Bacteria.
DR   OrthoDB; 9807519at2; -.
DR   Proteomes; UP000003448; Unassembled WGS sequence.
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; -; 2.
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; 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   PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR   Pfam; PF16499; Melibiase_2; 2.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   Pfam; PF14200; RicinB_lectin_2; 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; PS50231; RICIN_B_LECTIN; 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:UP000003448};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          468..606
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   608 AA;  65708 MW;  AE1D5BF7E95A62DC CRC64;
     MTLVLARSTA RRMAGLTALV VLLAVGLTVI SGKPAAAWDN GTADTPPMGW NSYDSFNWRV
     TESDVRANAD YMRDNLRQHG WEYIVIDWAW YYPGQHNNSP NQDANLNPRL RMDANGRLLP
     DTTRFPSAAG TNGFKPLADY VHDQGLKFGV HLMRGIPRQA VADNVPILGT NCRANQINNS
     TTAAWLNLMW GLNMSNACAQ AYLDSVFQLL ASWGVDFVKV DDIAAPTYRQ AEVEGYRTAI
     QHSGRPMVLS LSPGATPLSS GAHVRDNAHM WRIVNDLWDN WSSLDALFDQ LRNWTPYRTT
     GAWPDPDMIP IGRLSKYGPV GSPRYSGLTA DEQRTLMSLW AINRAPLMWG GNLVENRAAE
     LALMTNAAVL AVDQNSANNR QLVGGTRQVW TADVPGSDHR YVALLNRESA TANVSVNLAD
     LGIGSATVTD LWSGASLGTV TGTLTRSLPA HGSGLYRVAP LTTAPTPTTY TVAARHSGKL
     LDVSNASTAD GANVVQWGAN GQANQRWRFS DAGGGYSTVT SVSSGKCLDV FGGTGATADG
     VRVIQWACNG GTNQQWRVED LGTGYVRLVA RHSGKCLDVQ NAATADGAQA VQWTCGTGTS
     QQWRRTTV
//
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