AGALA_NEOFI
ID AGALA_NEOFI Reviewed; 532 AA.
AC A1DDD8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Probable alpha-galactosidase A;
DE EC=3.2.1.22;
DE AltName: Full=Melibiase A;
DE Flags: Precursor;
GN Name=aglA; ORFNames=NFIA_073100;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR EMBL; DS027696; EAW17395.1; -; Genomic_DNA.
DR RefSeq; XP_001259292.1; XM_001259291.1.
DR AlphaFoldDB; A1DDD8; -.
DR SMR; A1DDD8; -.
DR STRING; 36630.CADNFIAP00006638; -.
DR EnsemblFungi; EAW17395; EAW17395; NFIA_073100.
DR GeneID; 4586353; -.
DR KEGG; nfi:NFIA_073100; -.
DR VEuPathDB; FungiDB:NFIA_073100; -.
DR eggNOG; KOG2366; Eukaryota.
DR HOGENOM; CLU_013093_3_3_1; -.
DR OMA; NWARFMC; -.
DR OrthoDB; 964130at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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; 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; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lectin;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..532
FT /note="Probable alpha-galactosidase A"
FT /id="PRO_0000393212"
FT DOMAIN 410..531
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 210
FT /note="Proton donor"
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 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 124..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 427..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 466..478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 532 AA; 59159 MW; C30D4F7811422317 CRC64;
MYTTKSLLST LIPIMIPLSL GSVSSPNLLP TPPMGFNNWA RFMCDLNETL FLETASAMIS
TGLLEAGYNR LNLDDCWMAY DRAADSSLQW NTTKFPHGIP WLAYRLKTQG FHLGIYQDAG
NLTCGGYPGS FGYEALDAQT FAAWGIDYLK LDGCNVFPEH SRTLEEEYKA RYAHWHNVLR
QMHPPLIFSE SAPAYFADPA NLTSWYEVMD WVPAFGELAR HSTDILVYVG EGSAWDSIMV
NYHYNTLLAR YQRPGYFNDP DFLIPDHPGL TLEEKRSQFA LWASFSAPLI VSAYIPGLSG
EELAILRNEE LITVDQDVLG LQATLASRGE EVDVLTRSLA HGDQLLTVLN RGDGVPVVRV
PVEWMGLQRG CAYVVKNLWD GEVQVLEEEI VIRLNSHATQ VYRIALPEEC STVIPTGIVF
NTASGNCLTD ENGERVGFEA CRGSETQVWQ VSELGHLHPL SRTSHCLTAG SQASVQLCTG
QKNQQWTYEI TGNLKNEHTK MCLTEGTGIS QCGFERDSQV FGLPSGVDIK SS
