MEL6_YEASX
ID MEL6_YEASX Reviewed; 471 AA.
AC P41947;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Alpha-galactosidase 6;
DE EC=3.2.1.22;
DE AltName: Full=Alpha-D-galactoside galactohydrolase 6;
DE AltName: Full=Melibiase 6;
DE Flags: Precursor;
GN Name=MEL6;
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=7725791; DOI=10.1002/yea.320101205;
RA Turakainen H., Kristo P., Korhola M.;
RT "Consideration of the evolution of the Saccharomyces cerevisiae MEL gene
RT family on the basis of the nucleotide sequences of the genes and their
RT flanking regions.";
RL Yeast 10:1559-1568(1994).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; Z37510; CAA85739.1; -; Genomic_DNA.
DR PIR; S50312; S50312.
DR AlphaFoldDB; P41947; -.
DR SMR; P41947; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR SGD; S000029665; MEL6.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..471
FT /note="Alpha-galactosidase 6"
FT /id="PRO_0000001016"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000250"
FT DISULFID 121..151
FT /evidence="ECO:0000250"
FT DISULFID 221..237
FT /evidence="ECO:0000250"
FT DISULFID 223..230
FT /evidence="ECO:0000250"
SQ SEQUENCE 471 AA; 52113 MW; 5F6E1F325552AB54 CRC64;
MFAFYFLTAC ISLKGVFGVS PSYNGLGLTP QMGWDNWNTF ACDVSEQLLL DTADRISDLG
LKDMGYKYVI LDDCWSSGRD SDGFLVADKH KFPNGMGHVA DHLHNNSFLF GMYSSAGEYT
CAGYPGSLGR EEEDAQFFAN NRVDYLKYDN CYNKGQFGTP DVSYHRYKAM SDALNKTGRP
IFYSLCNWGQ DLTFYWGSGI ANSWRMSGDI TAEFTRPDSR CPCDGDEYDC KYAGFHCSIM
NILNKAAPMG QNAGVGGWND LDNLEVGVGN LTDDEEKAHF SMWAMVKSPL IIGADVNHLK
ASSYSIYSQA SVIAINQDPK GIPATRVWRY YVSDTDEYGQ GEIQMWSGPL DNGDQVVALL
NGGSVARPMN TTLEEIFFDS NLGSKELTST WDIYDLWANR VDNSTASAIL EQNKAATGIL
YNATEQSYKD GLSKNDTRLF GQKIGSLSPN AILNTTVPAH GIAFYRLRPS A