AGALA_ASPNG
ID AGALA_ASPNG Reviewed; 545 AA.
AC P28351;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Alpha-galactosidase A;
DE EC=3.2.1.22;
DE AltName: Full=Melibiase A;
DE Flags: Precursor;
GN Name=aglA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 32-59.
RC STRAIN=ATCC 9089 / N402;
RX PubMed=1320186; DOI=10.1007/bf00265437;
RA den Herder I.F., Rosell A.M.M., van Zuilen C.M., Punt P.J.,
RA van den Hondel C.A.M.J.J.;
RT "Cloning and expression of a member of the Aspergillus niger gene family
RT encoding alpha-galactosidase.";
RL Mol. Gen. Genet. 233:404-410(1992).
RN [2]
RP INDUCTION.
RX PubMed=10347026; DOI=10.1128/aem.65.6.2453-2460.1999;
RA de Vries R.P., van den Broeck H.C., Dekkers E., Manzanares P.,
RA de Graaff L.H., Visser J.;
RT "Differential expression of three alpha-galactosidase genes and a single
RT beta-galactosidase gene from Aspergillus niger.";
RL Appl. Environ. Microbiol. 65:2453-2460(1999).
CC -!- FUNCTION: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC more complex molecules such as oligosaccharides and polysaccharides.
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.
CC -!- INDUCTION: Expressed on galactose and galactosecontaining
CC oligosaccharides (lactose, melibiose, raffinose, and stachyose) and
CC polysaccharides (pectin, xylan, gum arabic, gum karaya, and locust bean
CC gum). {ECO:0000269|PubMed:10347026}.
CC -!- PTM: A C-terminal Ser/Thr-rich region may provide possible sites for O-
CC glycosylation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X63348; CAA44950.1; -; Genomic_DNA.
DR PIR; S23582; S23582.
DR AlphaFoldDB; P28351; -.
DR SMR; P28351; -.
DR STRING; 5061.CADANGAP00004923; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR CLAE; MEL27A_ASPNG; -.
DR GlyConnect; 42; 6 N-Linked glycans.
DR VEuPathDB; FungiDB:An06g00170; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1114396; -.
DR VEuPathDB; FungiDB:ATCC64974_96720; -.
DR VEuPathDB; FungiDB:M747DRAFT_296456; -.
DR eggNOG; KOG2366; Eukaryota.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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 CDD; cd00161; RICIN; 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 InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR11452; PTHR11452; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Lectin; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:1320186"
FT CHAIN 32..545
FT /note="Alpha-galactosidase A"
FT /id="PRO_0000000999"
FT DOMAIN 421..518
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 134..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 438..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 477..490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 545 AA; 60148 MW; 2DC5A710CE95D59C CRC64;
MIQGLESIMN QGTKRILLAA TLAATPWQVY GSIEQPSLLP TPPMGFNNWA RFMCDLNETL
FTETADTMAA NGLRDAGYNR INLDDCWMAY QRSDNGSLQW NTTKFPHGLP WLAKYVKAKG
FHFGIYEDSG NMTCGGYPGS YNHEEQDANT FASWGIDYLK LDGCNVYATQ GRTLEEEYKQ
RYGHWHQVLS KMQHPLIFSE SAPAYFAGTD NNTDWYTVMD WVPIYGELAR HSTDILVYSG
AGSAWDSIMN NYNYNTLLAR YQRPGYFNDP DFLIPDHPGL TADEKRSHFA LWASFSAPLI
ISAYIPALSK DEIAFLTNEA LIAVNQDPLA QQATLASRDD TLDILTRSLA NGDRLLTVLN
KGNTTVTRDI PVQWLGLTET DCTYTAEDLW DGKTQKISDH IKIELASHAT AVFRLSLPQG
CSSVVPTGLV FNTASGNCLT AASNSSVAFQ SCNGETSQIW QVTPSGVIRP VSQTTQCLAA
DGNLVKLQAC DSTDSDGQKW TYPVTGNLKN AKTDGCLTEG SVQMKSCLYE RDGQVFGLPS
GVQLA
