AGALD_ASPOR
ID AGALD_ASPOR Reviewed; 657 AA.
AC Q2UI87;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 77.
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=AO090023000151;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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=BAE58728.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007157; BAE58728.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001820730.2; XM_001820678.2.
DR AlphaFoldDB; Q2UI87; -.
DR SMR; Q2UI87; -.
DR STRING; 510516.Q2UI87; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR GeneID; 5992732; -.
DR KEGG; aor:AO090023000151; -.
DR VEuPathDB; FungiDB:AO090023000151; -.
DR Proteomes; UP000006564; Chromosome 3.
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..657
FT /note="Probable alpha-galactosidase D"
FT /id="PRO_0000395073"
FT ACT_SITE 155
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 200..204
FT /ligand="substrate"
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 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
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 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..157
FT /evidence="ECO:0000250"
SQ SEQUENCE 657 AA; 71140 MW; 50917D2103A5E8DF CRC64;
MLPKIFYLSL LPAALGHPHL QPRLDNGLAR TPQMGWNTYN HYSCSPNETI VRSNAQALVD
LGLASLGYRY VTTDCGWTVA DRLSDGSLTW NETLFPKGFP ALGKYLHDLD LLFGVYQDSG
IKLCGSPPDN VGSLYHEDQD ARTFASWEVD SLKYDNCYSD AATGYPNVNY EPSTSPQPRF
ANMSRALAAQ NRSMVFQVCE WGIDFPARWA PALGHSWRIG NDIIPHWRAI YRTLNQAVPQ
TSFAGPGQWP DLDMLFVGND ILSIPEEQTH FSLWAILKSP LTIGAALKDD NTSINDESLQ
ILKQEEVIGY NQDSLGVSAS LRRRWTEEGY EVWSGPLSGG RTVAALINWK DEARELTLDL
PDIGLQFAGT VKNIWDGTTA QNVKTSYTAK VQSHGTILLE LQDTTASGQY PTDTFATSTD
SSTTFESIYG VTTSFRYNIT VKLSEASSSG DVNIQSTASN KTITAQVSAS GTEASAQIPL
LAGSSNSITI VSPQSVDAIT ITPPNGTYFP NTAFTTTGDA DTVSCGAGYC QPVGSKIGNI
STNGTARAVI PATAGTKYLA IDYINNDVAF DSAWDWGSNS RNLTVSVNGN KPVRIEVPLS
GQHSELFGPG KGWWDTATIG VLTEGWKDGD NDVVIGNEGG ESGFTSYGPD FVGLRVL
