AGALB_ASPNC
ID AGALB_ASPNC Reviewed; 443 AA.
AC A2QEJ9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Probable alpha-galactosidase B;
DE EC=3.2.1.22;
DE AltName: Full=Melibiase B;
DE Flags: Precursor;
GN Name=aglB; ORFNames=An02g11150;
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:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR EMBL; AM270028; CAK44445.1; -; Genomic_DNA.
DR RefSeq; XP_001400244.1; XM_001400207.2.
DR AlphaFoldDB; A2QEJ9; -.
DR SMR; A2QEJ9; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR PaxDb; A2QEJ9; -.
DR EnsemblFungi; CAK44445; CAK44445; An02g11150.
DR GeneID; 4979651; -.
DR KEGG; ang:ANI_1_1552024; -.
DR VEuPathDB; FungiDB:An02g11150; -.
DR HOGENOM; CLU_013093_2_2_1; -.
DR Proteomes; UP000006706; Chromosome 4R.
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; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR PANTHER; PTHR11452; PTHR11452; 1.
DR Pfam; PF16499; Melibiase_2; 2.
DR Pfam; PF17801; Melibiase_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..443
FT /note="Probable alpha-galactosidase B"
FT /id="PRO_5000219645"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 243
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 221..225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..71
FT /evidence="ECO:0000250"
FT DISULFID 121..151
FT /evidence="ECO:0000250"
SQ SEQUENCE 443 AA; 48827 MW; D730DE6BCC5231E1 CRC64;
MRWLLTSSAL LVPAAALVRP DGVGRTPALG WNSWNAYSCD IDADKIVTAA NEVVNLGLKD
LGYEYINIDD CWSVKSGRNT TTKRIIPDPD KFPNGISGVA DQVHALGLKL GIYSSAGLTT
CAGYPASLGY EEIDAQSFAE WGIDYLKYDN CGVPTNLTDQ YTYCVPDSTD GSNYPNGTCV
NLTDAAPQGY DWATSTTAKR YQRMRDALLS VNRTILYSLC DWGQADVNAW GNATGNSWRM
SGDITATWSR IAEIANENSF LMNYANFWGY PDPDMLEVGN GNLTLPENRA HFALWAMMKA
PLIIGTPLDS IDTSHLTILS NKPLLTFHQD AVIGRPAYPY KWGYNPDWTF DPEHPAEYWS
GPTSSGEVFV LMLNSEGEVK TRSAVWEEVP ELKDRGTKKN SKEKKGFKVT DAWTGKDLGC
VKDKYEVKLQ AHDVAVLVVG GQC
