MEL1_YEASX
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 03-AUG-2022, entry version 118.
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}.
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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 PDBsum; 3LRK; -.
DR PDBsum; 3LRL; -.
DR PDBsum; 3LRM; -.
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 CLAE; MEL27A_YEAST; -.
DR iPTMnet; P04824; -.
DR PRIDE; 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:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.20.70; -; 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; IPR006215; Glyco_hydro_melibiase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR PANTHER; PTHR11452; PTHR11452; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR PRINTS; PR00748; MELIBIASE.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
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 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
