ID   AGALD_ASPTN             Reviewed;         655 AA.
AC   Q0CVX4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 61.
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=ATEG_02160;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476596; EAU37122.1; -; Genomic_DNA.
DR   RefSeq; XP_001211338.1; XM_001211338.1.
DR   AlphaFoldDB; Q0CVX4; -.
DR   SMR; Q0CVX4; -.
DR   STRING; 341663.Q0CVX4; -.
DR   GeneID; 4317058; -.
DR   eggNOG; KOG2366; Eukaryota.
DR   OrthoDB; 964130at2759; -.
DR   Proteomes; UP000007963; 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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..655
FT                   /note="Probable alpha-galactosidase D"
FT                   /id="PRO_0000395074"
FT   ACT_SITE        151
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         196..200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        540
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        579
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        126..153
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   655 AA;  71135 MW;  B947FFC92E244CDD CRC64;
     MASVIALSLL LPAAFAADHS PLRARLQDGL ARTPQMGWNT YNHYNCYPDE EIFRSNAKAL
     VDFGLADLGY RYATIDCGWT LTERLANGSL TWNATRFPSG FPAIADYLHD LGLLFGVYGD
     AGIKLCGPSD EHEEQDAQTF AAWGADSLKY DNCFSEASLG YPNVEYAPSS PLKPRYEVMS
     NALQKLDRPI LFQICEWGID FPALWAPALG HSWRIGNDII PAWRSVFRTL NQAVPQTDFA
     GPGQWPDLDM LMVGNGVYSV PEEETHFSLW AILKSPLIIG SALKDATTEI NSESLRILKQ
     KAVIGYNQDK LGVSASLRRR WTDQGYEVWS GPLSNGRTVA AVINWRGEAR DLTLDLPDIG
     LQSAGLVKNI WAGSTSRNVQ TSYTARVEGH GTMLLELRDT VPAGVYPKKI FGSSRGQGTV
     FKSVYAGSTS ENYTLAINFA KTIPSASKIT VQVGANRQKL SIAVPPSRQQ VTATIPLVAG
     SNNTITISHS HPITAIQVTS PNGTYYPATQ FSLTGAARHE TCGEGFCQPV GSKVSYLSPN
     STARGVIPAS AGTKYVEIDY INNEVAFSSS WGWGANSRNL TISLNGGEPV RLEVPLSGRH
     SELFGPGKGW WDTATLGVSV DGWKEGDNEV VVGNVNGEKG FQPYAADFVG LRVFD