ID MEL1_YEASX Reviewed; 471 AA. AC P04824; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 02-SEP-2026, entry version 132. DE RecName: Full=Alpha-galactosidase 1; DE EC=3.2.1.22; DE AltName: Full=Alpha-D-galactoside galactohydrolase 1; DE AltName: Full=Melibiase 1; DE Flags: Precursor; GN Name=MEL1; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2997745; DOI=10.1093/nar/13.20.7257; RA Liljestroem P.L.; RT "The nucleotide sequence of the yeast MEL1 gene."; RL Nucleic Acids Res. 13:7257-7268(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Carlsbergensis; RX PubMed=3000884; DOI=10.1016/0378-1119(85)90188-x; RA Sumner-Smith M., Bozzato R.P., Skipper N., Davies R.W., Hopper J.E.; RT "Analysis of the inducible MEL1 gene of Saccharomyces carlsbergensis and RT its secreted product, alpha-galactosidase (melibiase)."; RL Gene 36:333-340(1985). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) ALONE AND IN COMPLEX WITH MELIBIOSE RP AND RAFFINOSE, SUBCELLULAR LOCATION, SUBUNIT, ACTIVE SITE, RP SUBSTRATE-BINDING SITES, GLYCOSYLATION AT ASN-105; ASN-175; ASN-270; RP ASN-370; ASN-403 AND ASN-422, AND DISULFIDE BONDS. RX PubMed=20592022; DOI=10.1074/jbc.m110.144584; RA Fernandez-Leiro R., Pereira-Rodriguez A., Cerdan M.E., Becerra M., RA Sanz-Aparicio J.; RT "Structural analysis of Saccharomyces cerevisiae alpha-galactosidase and RT its complexes with natural substrates reveals new insights into substrate RT specificity of GH27 glycosidases."; RL J. Biol. Chem. 285:28020-28033(2010). 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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20592022}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20592022}. CC -!- INDUCTION: Induced by galactose and melibiose and repressed by glucose. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {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; X03102; CAA26888.1; -; Genomic_DNA. DR EMBL; M10604; AAA34770.1; -; Genomic_DNA. DR PIR; A00897; GBBYAG. DR PDB; 3LRK; X-ray; 1.95 A; A=1-471. DR PDB; 3LRL; X-ray; 2.40 A; A=1-471. DR PDB; 3LRM; X-ray; 2.70 A; A/B/C/D=1-471. DR AlphaFoldDB; P04824; -. DR SMR; P04824; -. DR DIP; DIP-1369N; -. DR IntAct; P04824; 1. DR MINT; P04824; -. DR CAZy; GH27; Glycoside Hydrolase Family 27. DR GlyCosmos; P04824; 9 sites, No reported glycans. DR iPTMnet; P04824; -. DR SGD; S000029662; MEL1. DR BRENDA; 3.2.1.22; 984. DR EvolutionaryTrace; P04824; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-ARBA. DR CDD; cd14792; GH27; 1. DR FunFam; 3.20.20.70:FF:000202; Alpha-galactosidase; 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; IPR006215; Glyco_hydro_melibiase. DR InterPro; IPR041233; Melibiase_C. DR PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE MEL1; 1. DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1. DR Pfam; PF16499; Melibiase_2; 1. DR Pfam; PF17801; Melibiase_C; 1. DR PRINTS; PR00740; GLHYDRLASE27. DR PRINTS; PR00748; MELIBIASE. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1. DR PDBsum; 3LRK; -. DR PDBsum; 3LRL; -. DR PDBsum; 3LRM; -. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; KW Secreted; Signal. FT SIGNAL 1..18 FT CHAIN 19..471 FT /note="Alpha-galactosidase 1" FT /id="PRO_0000001013" FT ACT_SITE 149 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:20592022" FT ACT_SITE 209 FT /note="Proton donor" FT /evidence="ECO:0000269|PubMed:20592022" FT BINDING 72 FT /ligand="substrate" FT BINDING 73 FT /ligand="substrate" FT BINDING 147 FT /ligand="substrate" FT BINDING 205 FT /ligand="substrate" FT BINDING 251 FT /ligand="substrate" FT CARBOHYD 105 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20592022" FT CARBOHYD 175 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20592022" FT CARBOHYD 270 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20592022" FT CARBOHYD 370 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20592022" FT CARBOHYD 403 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20592022" FT CARBOHYD 413 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 422 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20592022" FT CARBOHYD 435 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 454 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 42..74 FT /evidence="ECO:0000269|PubMed:20592022" FT DISULFID 121..151 FT /evidence="ECO:0000269|PubMed:20592022" FT DISULFID 221..237 FT /evidence="ECO:0000269|PubMed:20592022" FT DISULFID 223..230 FT /evidence="ECO:0000269|PubMed:20592022" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 32..36 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 37..40 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 46..58 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:3LRK" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 96..105 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 109..119 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 131..140 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 145..149 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 160..177 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 182..185 FT /evidence="ECO:0007829|PDB:3LRK" FT TURN 188..192 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 193..196 FT /evidence="ECO:0007829|PDB:3LRK" FT TURN 198..200 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 202..205 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 239..246 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 247..252 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 257..260 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 273..285 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 301..307 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 310..316 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 325..331 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 342..349 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 355..361 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 367..371 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 373..376 FT /evidence="ECO:0007829|PDB:3LRK" FT TURN 377..379 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 385..388 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 391..395 FT /evidence="ECO:0007829|PDB:3LRK" FT TURN 396..399 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 400..402 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 403..410 FT /evidence="ECO:0007829|PDB:3LRK" FT TURN 417..419 FT /evidence="ECO:0007829|PDB:3LRK" FT TURN 423..425 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 428..433 FT /evidence="ECO:0007829|PDB:3LRK" FT HELIX 437..440 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 442..447 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 453..457 FT /evidence="ECO:0007829|PDB:3LRK" FT STRAND 461..469 FT /evidence="ECO:0007829|PDB:3LRK" SQ SEQUENCE 471 AA; 52102 MW; 7A2E265A6BA09DBD CRC64; MFAFYFLTAC ISLKGVFGVS PSYNGLGLTP QMGWDNWNTF ACDVSEQLLL DTADRISDLG LKDMGYKYII LDDCWSSGRD SDGFLVADEQ KFPNGMGHVA DHLHNNSFLF GMYSSAGEYT CAGYPGSLGR EEEDAQFFAN NRVDYLKYDN CYNKGQFGTP EISYHRYKAM SDALNKTGRP IFYSLCNWGQ DLTFYWGSGI ANSWRMSGDV TAEFTRPDSR CPCDGDEYDC KYAGFHCSIM NILNKAAPMG QNAGVGGWND LDNLEVGVGN LTDDEEKAHF SMWAMVKSPL IIGANVNNLK ASSYSIYSQA SVIAINQDSN GIPATRVWRY YVSDTDEYGQ GEIQMWSGPL DNGDQVVALL NGGSVSRPMN TTLEEIFFDS NLGSKKLTST WDIYDLWANR VDNSTASAIL GRNKTATGIL YNATEQSYKD GLSKNDTRLF GQKIGSLSPN AILNTTVPAH GIAFYRLRPS S //