ID D9SZ70_MICAI Unreviewed; 551 AA.
AC D9SZ70;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 OrderedLocusNames=Micau_3680 {ECO:0000313|EMBL:ADL47206.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL47206.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL47206.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) 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; CP002162; ADL47206.1; -; Genomic_DNA.
DR RefSeq; WP_013286830.1; NC_014391.1.
DR AlphaFoldDB; D9SZ70; -.
DR STRING; 644283.Micau_3680; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR KEGG; mau:Micau_3680; -.
DR eggNOG; COG3345; Bacteria.
DR HOGENOM; CLU_013093_3_3_11; -.
DR OrthoDB; 9807519at2; -.
DR Proteomes; UP000001908; Chromosome.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; -; 3.
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 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.
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 Lectin {ECO:0000313|EMBL:ADL47206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..551
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003128596"
FT DOMAIN 425..551
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 551 AA; 58823 MW; 95F1E09E2DD8A6BD CRC64;
MRRWTRRTLA VLGVAAVALA ATVTDQAVAP RPARALDNGV ARTPPMGWNT WNTFGCNINE
TLIRQTADAI VSNGLRDLGY KYVVVDDCWF DPNRDSQGNL QAHPQRFPSG MKSLGDYLHA
RGLLFGIYQV PLDKTCAQVG GAFPGATGSL NHEYQDARQF AAWGVDYLKY DWCSSTGTIN
DQVARFGIMR DALASTGRPI VYSINPNSYH AKTGPQRNWS DVANLWRTTE DITNAWNTGQ
TNGYPMGIQN IVDVTVPLAG YAAPGGFNDP DMLEVGRGGM NDTEMRSHFA LWAVLAAPLM
MGNDVRSANA ATLAILRNAN LVAINQDTLG RQAAQVSFDG TRRVLAKPLA NGDVAVALFN
QGGSTTTVST TAAAVGKSGN SFTLRDAWTD ATSTSTGTIS ASVPAHGTVV YRVSGGGTTT
PPPVPTTFRL RSESSGRCLD VDNAGTANGT GTLIWDCHNN ANQQFTANGQ ALQVLGKCLD
VPTNATAGTR VQIWDCNGGT NQQWTINGNG TVSNGRFPSL CLDVDNAGTA NGTRVIVWTC
HGNANQRWSR A
//
