ID M7SY26_EUTLA Unreviewed; 749 AA.
AC M7SY26;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
DE EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
GN ORFNames=UCREL1_3832 {ECO:0000313|EMBL:EMR69177.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR69177.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- FUNCTION: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC more complex molecules such as oligosaccharides and polysaccharides.
CC {ECO:0000256|PIRNR:PIRNR005536}.
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|ARBA:ARBA00001255,
CC ECO:0000256|PIRNR:PIRNR005536};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase.
CC {ECO:0000256|PIRNR:PIRNR005536}.
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DR EMBL; KB706127; EMR69177.1; -; Genomic_DNA.
DR RefSeq; XP_007791758.1; XM_007793567.1.
DR AlphaFoldDB; M7SY26; -.
DR STRING; 1287681.M7SY26; -.
DR KEGG; ela:UCREL1_3832; -.
DR eggNOG; ENOG502QWG1; Eukaryota.
DR HOGENOM; CLU_009640_2_1_1; -.
DR OMA; WEGIYFD; -.
DR OrthoDB; 2194479at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd14791; GH36; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.70.98.60; alpha-galactosidase from lactobacil brevis; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR038417; Alpga-gal_N_sf.
DR InterPro; IPR002252; Glyco_hydro_36.
DR InterPro; IPR031705; Glyco_hydro_36_C.
DR InterPro; IPR031704; Glyco_hydro_36_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE C-RELATED; 1.
DR PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR Pfam; PF16874; Glyco_hydro_36C; 1.
DR Pfam; PF16875; Glyco_hydro_36N; 1.
DR Pfam; PF02065; Melibiase; 1.
DR PIRSF; PIRSF005536; Agal; 1.
DR PRINTS; PR00743; GLHYDRLASE36.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR005536};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005536};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..749
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004085231"
FT DOMAIN 90..303
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 670..744
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 507
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 569
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 385..386
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 505..509
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 547
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 569
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 749 AA; 83105 MW; A2164D5602BC4EB7 CRC64;
MFSNSTVRRL FAPATLALVL AYPVTAQNSS YNTGVVVDGK EFALNGNGVS YRFYADETGD
LISTHFGGPV TESIITPPLP DPNGWVGLPG RVRREYPDLG RGDFRIPAFQ IRQSEGYTVS
DFQYKSHDVI QGKPALPGLP ATFGSEGEVT TLVVHLYDNY SSVAADLSYS IFPEHDAIVR
SVNITNEGPD DITLEKISSL SVDLPYEDLD MIELRGDWAR EAQRVRRKVE YGTQGFGSLT
GYSSHLHNPF LALLSPTTTE SHGEAWGFSL VYSGSFSVDV EKGSQGFTRA ILGLNPYQFS
WSLGPGETFT SPEAVSVYSD SGVGGVSRKF HRLYRDNLIK SHYAKEDRPV LLNSWEGAYF
DFNESVIYDL ADASADLGIK LFVMDDGWFG DKYPRLSDNS SLGDWVVNKD RFPEGLGPLV
DRITQLDAGN SSEKIRFGIW FEPEMVSPHS ELYDAHPDWA LHADGYPRTE RRNQLVLNVG
LPEVQDYIID SVSKILESAD ISYVKWDNNR GMHETASPNT SHSYILGLYH VFEVLTTRFP
DVLFEGCASG GGRFDPGMLQ YFPQIWTSDD TDGLERIAIQ FGTSLVYPPS TMGAHVSNVP
NHQTSRTTPF TFRAHVAMMG GSFGFELDPA DLDEDDKVLI PDLIALAEQL NPIVIQGDLW
RLNLPEESNW PAALFITPDG ESAVLFWFQV RANINHAAPF LRLQGLDPAA RYTVEGNATY
SGLTLMNIGL QYYFDGDYDS KVVLIEKAS
//
