ID W6Q5W7_PENRF Unreviewed; 746 AA.
AC W6Q5W7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=PROQFM164_S02g001526 {ECO:0000313|EMBL:CDM31376.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM31376.1};
RN [1] {ECO:0000313|EMBL:CDM31376.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM31376.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family.
CC {ECO:0000256|ARBA:ARBA00006202}.
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DR EMBL; HG792016; CDM31376.1; -; Genomic_DNA.
DR AlphaFoldDB; W6Q5W7; -.
DR STRING; 1365484.W6Q5W7; -.
DR OMA; WEGIYFD; -.
DR OrthoDB; 2194479at2759; -.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR005536};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005536};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..746
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004879932"
FT DOMAIN 87..301
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 668..743
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 505
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 567
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 383..384
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 503..507
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 545
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 567
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 746 AA; 81853 MW; D57866999A7B6A9D CRC64;
MVHLSRGVVA TCLTLLAHSS GITAEESSTN PIVADGTSFA LNGNNVAYRI HVDNTTGDLL
GDHFGGSVGA HIPLEVVGDV HGWNGYIGRV RREFPDQGRG DFRTPAIRIR QSQGYTVSEF
QYKSYKIIPG KPALPGLPAT TGTEEDVSTL VISLYDKYSD VGADLSYSIF PKYDAIVRSV
NITNHGKANI TIESLASLSV DLPFEDLDMI SLRGDWAREA HRERKKVTYG TQGFGSSTGY
SSHLHNPFLA LTEPSATESH GEVWGFSLVY TGSFSVNVEK GSQGFTRALL GFNPSQLSWN
LPPGETLTSP ECVSVYSKDG IGGMSRSLHR LYRKHLIKSK FATSDRPTLL NSWEGLYFDY
NQSSIYDLAK EAAEVGAKLF VLDDGWFGRE YPRLSDDAGL GDWIPNPDRF PDGLGPIVKN
ITDLKAANSS TNMRFGIWFE PEMVNPNSTL YNEHPDWALH AGPYPRTERR NQLVLNLALP
EVQDYIIKSV SDVLKSADIS YVKWDNNRGI HEMPSPATDH AYILGMYRVF DELTTQFPDI
LWEGCASGGG RFDPGVLQYF PQIWTSDNTD AIDRISIQLG TSLAYPPSAM GAHLSEVPNQ
QTGRTVPVAV RGHVAMMAGS FGLELDPAVM NAEDKAALPG LIALAEKVNP IVLTGDMWRL
NLPEDSNWPA VLFIAEDGQK AVLFVFQLAP NVAHSWPRVR LQGLDAQASY KIDGGVVYSG
GTLMNIGLQF PFKGDYGSQV VMLEKQ
//
