AGALA_ASPCL
ID AGALA_ASPCL Reviewed; 525 AA.
AC A1CBW8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=ACLA_016820;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027049; EAW13236.1; -; Genomic_DNA.
DR RefSeq; XP_001274662.1; XM_001274661.1.
DR AlphaFoldDB; A1CBW8; -.
DR SMR; A1CBW8; -.
DR STRING; 5057.CADACLAP00001524; -.
DR EnsemblFungi; EAW13236; EAW13236; ACLA_016820.
DR GeneID; 4706882; -.
DR KEGG; act:ACLA_016820; -.
DR VEuPathDB; FungiDB:ACLA_016820; -.
DR eggNOG; KOG2366; Eukaryota.
DR HOGENOM; CLU_013093_3_3_1; -.
DR OMA; NWARFMC; -.
DR OrthoDB; 964130at2759; -.
DR Proteomes; UP000006701; 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 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..525
FT /note="Probable alpha-galactosidase A"
FT /id="PRO_0000393213"
FT DOMAIN 402..525
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT ACT_SITE 148
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 120..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 422..434
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 459..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 525 AA; 57347 MW; DBDD564471DEF811 CRC64;
MHPSMTLLAI LPPLVRASIG NPHLLPTPPM GFNNWARFMC NLNESLFLDT AAAMLDTGLH
AAGYTRLNLD DCWMASHRAP NGSLPWDPTK FPHSLPWLSA QLRSLGFSLG IYQDAGNVTC
GGYPGSYGFE ELDAHTFAEW GVDYLKLDGC NVSPAGAVSL ADEYRARYAR WHSVLGAMPH
PLVFSESAPA YFVDPQNATA WYGVMDWVPA YGELARHSTD ILVYEGEGSA WQSIMVNYRY
NTLLARYQRP GYFNDPDFLI ADHPGLSLVE KRSHFALWAS FGAPLIISAD VPGLSKEVIA
VLTNADLIRV DQDALGLQAT LASRSEHLDV LTRSLDGGDR LVTILNRGDG GLAVKVPVGW
MGLQRCAYQA KNLWDGEIQE IEEDIEVQLD SHATEVFRVS LPPDCPMVIP TGIVFNTASG
NCLTDGEALA FEPCRGQDLQ VWQVEESGIL RPLSRTSHCL TAIGDNVVVK PCTGRPGQRW
TYHITGNLQN QHTGACLTEG TGIDVCGFEL DSQVFGLPSG VDIEA
