ID AGALA_ASPNG Reviewed; 545 AA. AC P28351; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 02-SEP-2026, entry version 127. DE RecName: Full=Alpha-galactosidase A; DE EC=3.2.1.22; DE AltName: Full=Melibiase A; DE Flags: Precursor; GN Name=aglA; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati. OX NCBI_TaxID=5061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 32-59. RC STRAIN=ATCC 9089 / N402; RX PubMed=1320186; DOI=10.1007/bf00265437; RA den Herder I.F., Rosell A.M.M., van Zuilen C.M., Punt P.J., RA van den Hondel C.A.M.J.J.; RT "Cloning and expression of a member of the Aspergillus niger gene family RT encoding alpha-galactosidase."; RL Mol. Gen. Genet. 233:404-410(1992). RN [2] RP INDUCTION. RX PubMed=10347026; DOI=10.1128/aem.65.6.2453-2460.1999; RA de Vries R.P., van den Broeck H.C., Dekkers E., Manzanares P., RA de Graaff L.H., Visser J.; RT "Differential expression of three alpha-galactosidase genes and a single RT beta-galactosidase gene from Aspergillus niger."; RL Appl. Environ. Microbiol. 65:2453-2460(1999). CC -!- FUNCTION: Hydrolyzes a variety of simple alpha-D-galactoside as well as CC more complex molecules such as oligosaccharides and polysaccharides. 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 -!- SUBCELLULAR LOCATION: Secreted. CC -!- INDUCTION: Expressed on galactose and galactosecontaining CC oligosaccharides (lactose, melibiose, raffinose, and stachyose) and CC polysaccharides (pectin, xylan, gum arabic, gum karaya, and locust bean CC gum). {ECO:0000269|PubMed:10347026}. CC -!- PTM: A C-terminal Ser/Thr-rich region may provide possible sites for O- CC glycosylation. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X63348; CAA44950.1; -; Genomic_DNA. DR PIR; S23582; S23582. DR AlphaFoldDB; P28351; -. DR SMR; P28351; -. DR CAZy; GH27; Glycoside Hydrolase Family 27. DR GlyConnect; P28351; 6 N-Linked glycans. DR GlyCosmos; P28351; 7 sites, 9 glycans. DR VEuPathDB; FungiDB:An06g00170; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1114396; -. DR VEuPathDB; FungiDB:ATCC64974_96720; -. DR VEuPathDB; FungiDB:M747DRAFT_296456; -. DR eggNOG; KOG2366; Eukaryota. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd23425; beta-trefoil_Ricin_AglA; 1. DR CDD; cd14792; GH27; 1. DR FunFam; 3.20.20.70:FF:000177; Alpha-galactosidase; 1. DR FunFam; 2.60.40.1180:FF:000056; Alpha-galactosidase A; 1. DR FunFam; 2.80.10.50:FF:000077; Alpha-galactosidase A; 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; IPR017853; GH_hydrolase_sf. DR InterPro; IPR002241; Glyco_hydro_27. DR InterPro; IPR000111; Glyco_hydro_27/36_CS. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR041233; Melibiase_C. DR InterPro; IPR035992; Ricin_B-like_lectins. DR InterPro; IPR000772; Ricin_B_lectin. DR PANTHER; PTHR11452:SF91; ALPHA-GALACTOSIDASE A-RELATED; 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 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Lectin; Secreted; Signal. FT SIGNAL 1..31 FT /evidence="ECO:0000269|PubMed:1320186" FT CHAIN 32..545 FT /note="Alpha-galactosidase A" FT /id="PRO_0000000999" FT DOMAIN 421..518 FT /note="Ricin B-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT ACT_SITE 162 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 220 FT /note="Proton donor" FT /evidence="ECO:0000250" FT CARBOHYD 57 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 95 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 101 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 131 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 211 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 363 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 444 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 54..86 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 134..164 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 438..452 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 477..490 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" SQ SEQUENCE 545 AA; 60148 MW; 2DC5A710CE95D59C CRC64; MIQGLESIMN QGTKRILLAA TLAATPWQVY GSIEQPSLLP TPPMGFNNWA RFMCDLNETL FTETADTMAA NGLRDAGYNR INLDDCWMAY QRSDNGSLQW NTTKFPHGLP WLAKYVKAKG FHFGIYEDSG NMTCGGYPGS YNHEEQDANT FASWGIDYLK LDGCNVYATQ GRTLEEEYKQ RYGHWHQVLS KMQHPLIFSE SAPAYFAGTD NNTDWYTVMD WVPIYGELAR HSTDILVYSG AGSAWDSIMN NYNYNTLLAR YQRPGYFNDP DFLIPDHPGL TADEKRSHFA LWASFSAPLI ISAYIPALSK DEIAFLTNEA LIAVNQDPLA QQATLASRDD TLDILTRSLA NGDRLLTVLN KGNTTVTRDI PVQWLGLTET DCTYTAEDLW DGKTQKISDH IKIELASHAT AVFRLSLPQG CSSVVPTGLV FNTASGNCLT AASNSSVAFQ SCNGETSQIW QVTPSGVIRP VSQTTQCLAA DGNLVKLQAC DSTDSDGQKW TYPVTGNLKN AKTDGCLTEG SVQMKSCLYE RDGQVFGLPS GVQLA //