AGALD_ASPFU
ID AGALD_ASPFU Reviewed; 648 AA.
AC A4DA70;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 69.
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=AFUA_4G03585;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EBA27184.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAHF01000016; EBA27184.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001481538.1; XM_001481488.1.
DR AlphaFoldDB; A4DA70; -.
DR SMR; A4DA70; -.
DR STRING; 746128.CADAFUBP00009667; -.
DR GeneID; 5077090; -.
DR KEGG; afm:AFUA_4G03585; -.
DR eggNOG; KOG2366; Eukaryota.
DR HOGENOM; CLU_013093_3_0_1; -.
DR InParanoid; A4DA70; -.
DR OrthoDB; 964130at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004557; F:alpha-galactosidase activity; IBA:GO_Central.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR GO; GO:0046477; P:glycosylceramide catabolic process; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
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..648
FT /note="Probable alpha-galactosidase D"
FT /id="PRO_0000395072"
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 350
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; 70100 MW; DA34A68726860416 CRC64;
MEFIVSLLLL SPALVAGSLH SRIDNGLART PQMGWNSYNY YSCSPNEAII RSNAKALVDL
GLAELGYRYV TTDCGWSVAD RLPNGTLTWN ETLFPSGFPA MGEYLHELGL LFGVYGDSGT
KLCGSPPDQV GSLYHEEQDA KTFAEWGADS LKYDNCYSDA ATNYPNVNYE PSTSPRPRYE
IMSSALARVG RPILFQICEW GIDFPALWAP ALGNSWRIGN DIIPAWRSIF RTLNQAVPNT
DFAGPGQWAD LDMLYVGNGV FSLPEEQTHF SLWAILKSPL TIGAALKDDD TSISQASLEV
LKQKDVIGFN QDALGVSASL KRRWSDEGYE VWSGPLSGNR TVVAVINWRN ESRDLTLDLP
DVGLQYAQVA RNIWGKTVVR DVRTSYTAGV AGHGTILLEL QGTLPSGLYP AKIFAKSTGQ
RSTFESIYAA TTSANYELAI TFSRPSTETV TITTSSGQTV SISGKSGRIA LTAGSNTITI
QHKTPIESIQ ITPPTGTYYA NTVFNVTGSA KHTTCGSGCS PVGSKIGYLS PTSNAYTSIS
TTTAGSKYLA IDYINNEVAF SSSWGWGSNS RNLTVSVNDG APVRLEVPLS GRHSELYSPG
KGWWDTATLG VLTSGWKKGE NKVVFGNEGG EDGFQTYAAD FVGVRVLD
