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
//