AGALD_ASPNC
ID AGALD_ASPNC Reviewed; 660 AA.
AC A2R2S6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Probable alpha-galactosidase D;
DE EC=3.2.1.22;
DE AltName: Full=Melibiase D;
DE Flags: Precursor;
GN Name=aglD; ORFNames=An14g01800;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC more complex molecules such as oligosaccharides and polysaccharides.
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK46492.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM270315; CAK46492.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001400806.2; XM_001400769.2.
DR AlphaFoldDB; A2R2S6; -.
DR SMR; A2R2S6; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR PaxDb; A2R2S6; -.
DR EnsemblFungi; CAK46492; CAK46492; An14g01800.
DR GeneID; 4987036; -.
DR KEGG; ang:ANI_1_276124; -.
DR Proteomes; UP000006706; Chromosome 1R.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; IPR013780; Glyco_hydro_b.
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 SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..660
FT /note="Probable alpha-galactosidase D"
FT /id="PRO_5000220909"
FT ACT_SITE 155
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 200..204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
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 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..157
FT /evidence="ECO:0000250"
SQ SEQUENCE 660 AA; 71228 MW; A92D587C27009651 CRC64;
MLLHFILYAA LSSVVTSVSL QPRLQDGLAL TPQMGWNTYN HYSCSPNETI VQSNAQALVD
LGLSSLGYRY VTTDCGWTVA DRLPDGSLTW NDTLFPQGFP AMGDFLHDLG LLFGVYQDSG
ILLCGSPPNE TGSLYHEEQD ARTFASWNVD SLKYDNCYSD AATGYPNVNY APSTSPEPRF
ANMSHALLQQ NRTILFQICE WGISFPANWA PALGHSWRIG NDIIPDWRTI FRIINQAAPQ
TDVAGPGQWP DLDMLEVGNN IFSLPEEQTH FSLWAILKSP LIIGAALKDE LTAINDASLA
VLKQKDVIAF NQDALGKSAS LRRRWTEEGY EVWSGPLSNG RTVAAVINWH NESKDLTLDL
PDVGLQHAGT VKNIWDGTTA RDVLTSYTAT VAGHGTMLLE LQNTTAVGVY PRGVFGVSSG
QTTTFQNIYA VTTSAKYIIS VYFSQPASST ETITIGSNAN QSMISAQVPA SSTLVSAEIP
LTAGSSNTIT INTSIPIDAI HVTPPNGTYY PCTNFTLAGS TTLTTCGSGY CQPVGSKVGY
ISPSGTAKAT ISATTSGSKY LEIDWINNDI AFDSSWGWGS NSRNLTVTVN SEDPVRIEVP
LSGRHSELFG PGLGWWDTST LGLLTSGWKE GLNEVVVGNV GGDEGFQSYG ADFVGIRVLD
