AGALA_ASPTN
ID AGALA_ASPTN Reviewed; 529 AA.
AC Q0CPK2;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 66.
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=ATEG_04382;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU34829.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476599; EAU34829.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001213560.1; XM_001213560.1.
DR AlphaFoldDB; Q0CPK2; -.
DR SMR; Q0CPK2; -.
DR STRING; 341663.Q0CPK2; -.
DR EnsemblFungi; EAU34829; EAU34829; ATEG_04382.
DR GeneID; 4320194; -.
DR eggNOG; KOG2366; Eukaryota.
DR OrthoDB; 1510302at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..529
FT /note="Probable alpha-galactosidase A"
FT /id="PRO_0000393211"
FT DOMAIN 408..528
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 122..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 425..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 462..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 529 AA; 58367 MW; 8B378778EC0938D3 CRC64;
MKALFAAITM AHALLQTQAS LQNPNLLPTP PMGFNNWARF MCDLNETLFV ETADAMAANG
LLAAGYNWLN LDDCWMTHQR APNNSLMWNT TKFPRGLPWL GSYVKAKGFR FGIYEDAGNL
TCGGYPGSLG HEELDARTFA DWGVEYLKLD GCNVFPEGGR TSEQQYEHLY GLWHRILSGM
PHPLVFSESA PAYFANEKNL SDWYTVMDWV PRYGELARHS TDILVYAGEG SAWDSIMVNY
RYNTLVARYQ RPGYYNDPDF LIPDHPGLTM DEKKSHFGLW ASFAAPLIIS AYIPGLSEED
IGYLTNRDLI AVDQDPLAQQ ATLASRDDEV DVLTRSLADG SRLVSVLNRG NSSVQRVIPL
QWLGLNPGQR YQARNLWDGT EKRIRKDLTV TVRSHATEIY KFTGSNGRVD AVSTGIVFNT
ASGNCLTGDA AGVGFAPCTG GEKQIWQVRG SELRPLSLLG ECLTADGTRL SLRPCAGDEA
QMWSYHISGN LKSGHEGGCL TEGHGVASCG WELNSQVFGL PSGVRVSGY
