AGALA_ASPOR
ID AGALA_ASPOR Reviewed; 534 AA.
AC Q2UT06;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=AO090005000217;
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}.
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DR EMBL; AP007151; BAE55309.1; -; Genomic_DNA.
DR RefSeq; XP_001817311.1; XM_001817259.1.
DR AlphaFoldDB; Q2UT06; -.
DR SMR; Q2UT06; -.
DR STRING; 510516.Q2UT06; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR EnsemblFungi; BAE55309; BAE55309; AO090005000217.
DR GeneID; 5989256; -.
DR KEGG; aor:AO090005000217; -.
DR VEuPathDB; FungiDB:AO090005000217; -.
DR HOGENOM; CLU_013093_3_3_1; -.
DR OMA; NWARFMC; -.
DR Proteomes; UP000006564; Chromosome 1.
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;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..534
FT /note="Probable alpha-galactosidase A"
FT /id="PRO_0000393210"
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; 58739 MW; 64F2097EFD0C24E0 CRC64;
MRLITRWIPL ANALASTMPV QVVASIENPS LLPTPPMGFN NWARFMCDLN ETLFVETTDA
MASNGLLEAG YNRINLDDCW MNYDRAENGS LEWNVTKFPR GLPWLGQYVK SKGFNFGIYE
DSGNLTCGGY PGSEGYEEID AEIFAAWGID 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
