ID A0A5C3PH48_9APHY Unreviewed; 477 AA.
AC A0A5C3PH48;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|RuleBase:RU361168};
DE EC=3.2.1.22 {ECO:0000256|RuleBase:RU361168};
DE AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN ORFNames=K466DRAFT_43179 {ECO:0000313|EMBL:TFK89075.1};
OS Polyporus arcularius HHB13444.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=1314778 {ECO:0000313|EMBL:TFK89075.1, ECO:0000313|Proteomes:UP000308197};
RN [1] {ECO:0000313|EMBL:TFK89075.1, ECO:0000313|Proteomes:UP000308197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB13444 {ECO:0000313|EMBL:TFK89075.1,
RC ECO:0000313|Proteomes:UP000308197};
RX PubMed=30886374; DOI=.1038/s41559-019-0834-1;
RA Varga T., Krizsan K., Foldi C., Dima B., Sanchez-Garcia M.,
RA Sanchez-Ramirez S., Szollosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA Damon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA Grigoriev I.V., Vagvolgyi C., Papp T., Martin F.M., Miettinen O.,
RA Hibbett D.S., Nagy L.G.;
RT "Megaphylogeny resolves global patterns of mushroom evolution.";
RL Nat. Ecol. Evol. 3:668-678(2019).
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|RuleBase:RU361168};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC {ECO:0000256|ARBA:ARBA00009743, ECO:0000256|RuleBase:RU361168}.
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DR EMBL; ML211088; TFK89075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C3PH48; -.
DR STRING; 1314778.A0A5C3PH48; -.
DR InParanoid; A0A5C3PH48; -.
DR Proteomes; UP000308197; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14792; GH27; 1.
DR FunFam; 3.20.20.70:FF:000197; 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; IPR000254; CBD.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR017853; GH.
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 PANTHER; PTHR11452:SF61; ALPHA-GALACTOSIDASE B-RELATED; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361168};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361168};
KW Reference proteome {ECO:0000313|Proteomes:UP000308197};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..477
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5022752425"
FT DOMAIN 17..53
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 70..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..83
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 50835 MW; E7D9850EC7CC1147 CRC64;
MLLLYGSVFA ALLLSAVAES EFGQCGGTGW SGDTTCPSGW VCAALTAHYS QCVPGISSVA
STTASQSATR ATTTSAAPTA APTVGPSHAT GKTPALGWNS WNAYACDINE DKILAAANQF
VSLGLAKAGY QYVNIDDCWS VKTRDASTGR IVPDPDKFPS GISGVASQVH SLGLKFGIYS
DAGTQTCAGY PASLGNEELD AATFAEWGVD YLKYDNCNVP ANWSDASTPP GGDWYNSNSA
IRYRQMTAAL DATGRPFHFN LCIWGNANVW DWGARVGHSW RMSGDASASW SYITSIITTN
VQHLDSIDFY SHNDMDMMEI GNGDLTIQEQ RTHFAAWAFF KSPILLGTDL GQLNSTQLAI
ITNPELLAFH QDTTVGTPAR PFTPTSSAPT TSPPEFYSGR SVKGTHVFII NTGNATSKTF
DFAKVPGLGS GSYKLHDMWT GKDLGTFTKS HTSTVDTHDT AAFLVTPARH GADVDEE
//
