AGALA_ASPNC
ID AGALA_ASPNC Reviewed; 537 AA.
AC A2QL72;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=An06g00170;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270108; CAK44933.1; -; Genomic_DNA.
DR RefSeq; XP_001390845.1; XM_001390808.1.
DR AlphaFoldDB; A2QL72; -.
DR SMR; A2QL72; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR PaxDb; A2QL72; -.
DR EnsemblFungi; CAK44933; CAK44933; An06g00170.
DR GeneID; 4981013; -.
DR KEGG; ang:ANI_1_6054; -.
DR VEuPathDB; FungiDB:An06g00170; -.
DR HOGENOM; CLU_013093_3_3_1; -.
DR BRENDA; 3.2.1.49; 518.
DR Proteomes; UP000006706; Chromosome 8ER.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0015925; F:galactosidase activity; IDA:AspGD.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IMP:AspGD.
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; IPR000111; Glyco_hydro_27/36_CS.
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; PS00512; ALPHA_GALACTOSIDASE; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..537
FT /note="Probable alpha-galactosidase A"
FT /id="PRO_5000220032"
FT DOMAIN 413..537
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 126..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 430..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 469..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 537 AA; 59213 MW; F093FD8196C7F839 CRC64;
MNQGTKSILL AATLAAIPWQ VYGSIEQSSL LPIPPMGFNN WARFMCDLNE TLFTETADAM
AANGLRDAGY NRINLDDCWM AYQRSDNGSL QWNTTKFPHG LPWLAQYVKA KGFHFGIYED
SGNMTCGGYP GSYNHEEQDA NTFALWGIDY LKLDGCNVYA TQGRTLEEEY KQRYGHWHQV
LSKMQHPLIF SESAPAYFAG TDNNTDWYTV MDWVPIYGEL ARHSTDILVY SGAGSAWDSI
MNNYNYNTLL ARYQRPGYFN DPDFLIPDHP GLTADEKRSH FALWASFSAP LIISAYIPAL
SKDEIAFLTN EALIAVNQDP LAQQATFASR DNTLDILTRN LANGDRLLTV LNKGNTTVTR
DIPVQWLGLT ETDCTYTAED LWDGKTQKIS DHIKIELASH ATAVFRLGLP QGCSSVVPTG
LVFNTASGNC LTAASNSSVA FQSCNGETSQ IWQVTLSGVI RPVSQTTQCL AADGNSVKLQ
ACDSTDSDGQ NWTYAVTGNL KNAKTDGCLT EGSVQMKSCL YERDGQVFGL PSGVQLS
