ID   AGALD_NEOFI             Reviewed;         648 AA.
AC   A1D9S3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=NFIA_029860;
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; DS027693; EAW20554.1; -; Genomic_DNA.
DR   RefSeq; XP_001262451.1; XM_001262450.1.
DR   AlphaFoldDB; A1D9S3; -.
DR   SMR; A1D9S3; -.
DR   STRING; 36630.CADNFIAP00002758; -.
DR   EnsemblFungi; EAW20554; EAW20554; NFIA_029860.
DR   GeneID; 4589010; -.
DR   KEGG; nfi:NFIA_029860; -.
DR   VEuPathDB; FungiDB:NFIA_029860; -.
DR   eggNOG; KOG2366; Eukaryota.
DR   HOGENOM; CLU_013093_3_0_1; -.
DR   OMA; TLKYDNC; -.
DR   OrthoDB; 964130at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..648
FT                   /note="Probable alpha-galactosidase D"
FT                   /id="PRO_0000395076"
FT   ACT_SITE        154
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        505
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        572
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        123..156
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   648 AA;  70198 MW;  1539A806D1071EDB CRC64;
     MESIVWLLLL SPALVAGSLH PRIDNGLAKT PQMGWNSYNY YSCSPNEAIV RSNAKALVDL
     GLADLGYRYV TTDCGWSVAD RLPNGTLTWN ETLFPSGFPA MGKYLHELGL LFGVYGDSGT
     KLCGSPPDQV GSLYHEEQDA KTFAEWGADS LKYDNCYSDA ATNYPNVNYE PSTSPRPRYE
     IMSSALARVG RPILFQICEW GIDFPALWAP ALGSSWRIGN DIIPEWRSIF RTLNQAVPNT
     DFAGPGQWAD LDMLYVGNGV FSLPEEQTHF SLWAILKSPL TIGAALKDDD TSINQASLEV
     LKQKDVIGFN QDALGVSASL KRRWSDEGYE VWSGPLSGNR TVVAVINWRD ESRDLTLDLP
     DVGLQYAQVA RNIWGKTVVR DVRTSYTAGV AGHGTMLLEL QGTIPSGLYP AKIFAKSTDQ
     KTTFESIYAA TTSANYELAI TFSRPSTETV TITTSSGQTI SISGKSGRIA LTAGSNTITI
     QHKTPIESIQ ITPPTGTYYA NTVFNVTGSA KHTTCGSGCS PVGSKIGDLS PNSNAYTSIP
     ATTVGSKYLA IDYINNEVAF SSSWGWGSNS RNLTVSVNDG APVRLEVPLS GRHSELFSPG
     KGWWDTATLG VLTSGWKKGE NKVVFGNQGG EDGFQTYAAD FVGVRILD