ID   AGALA_ASPFN             Reviewed;         534 AA.
AC   B8MWJ5;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=AFLA_074520;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963472; EED56758.1; -; Genomic_DNA.
DR   RefSeq; XP_002372370.1; XM_002372329.1.
DR   AlphaFoldDB; B8MWJ5; -.
DR   SMR; B8MWJ5; -.
DR   STRING; 5059.CADAFLAP00000235; -.
DR   EnsemblFungi; EED56758; EED56758; AFLA_074520.
DR   VEuPathDB; FungiDB:AFLA_074520; -.
DR   eggNOG; KOG2366; Eukaryota.
DR   HOGENOM; CLU_013093_3_3_1; -.
DR   OMA; NWARFMC; -.
DR   Proteomes; UP000001875; 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; Secreted;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..534
FT                   /note="Probable alpha-galactosidase A"
FT                   /id="PRO_0000393208"
FT   DOMAIN          413..534
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   ACT_SITE        155
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        213
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
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        47..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        127..157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        430..443
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        468..481
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ   SEQUENCE   534 AA;  58727 MW;  C80E0A4805C82F1F CRC64;
     MRLITRWIPL ANALASTMPV QVVASIENPS LLPTPPMGFN NWARFMCDLN ETLFVETTDA
     MASNGLLEAG YNRINLDDCW MNYDRAENGS LEWNVTKFPR GLPWLGQYVK SKGFNFGIYE
     DSGNLTCGGY PGSEGYEEID AETFAAWGID YLKLDGCNVY PKEGRTLQEE YKYLYGNWHE
     ILSKMQQPLI FSESAPAYFS MTDNLTDWHT VMDWVPEYGE LARHSVDILV YSGEGSAWDS
     IMTNYKFNTL VARYQRPGYY NDPDFLIADH PGLSLDEKRS QFALWASFSA PLIISAHIPD
     LSSEDLEYLT NQALIAVDQD PLAQQATLAS RDGSLDVLTR NLADGSRLVT ILNHGSESIE
     TDISLDILGL STDCTYKAQD LWGGSTQTIK DAIRIKLNTH ATAVYKIDTD EKCSQVIPTG
     LIFNTASGKC LTGTSSSVGS ESCNGSKSQI WQIDASGVIR TLSEQSKCLT ADGKAISLQE
     CSENNGQKWS YAITGNLKNA DTGYCLTNGG GVSACGFETN SQVFGLPAGV HVAL