(data stored in ACNUC7421 zone)

SWISSPROT: A2Q7N1_ASPNC

ID   A2Q7N1_ASPNC            Unreviewed;       391 AA.
AC   A2Q7N1;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 69.
DE   RecName: Full=Alpha-galactosidase {ECO:0000256|RuleBase:RU361168};
DE            EC=3.2.1.22 {ECO:0000256|RuleBase:RU361168};
DE   AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN   ORFNames=An01g01320 {ECO:0000313|EMBL:CAK43504.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK43504.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
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., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.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   -!- 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         Evidence={ECO:0000256|RuleBase:RU361168};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC       {ECO:0000256|RuleBase:RU361168, ECO:0000256|SAAS:SAAS01073723}.
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DR   EMBL; AM269954; CAK43504.1; -; Genomic_DNA.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   PaxDb; A2Q7N1; -.
DR   EnsemblFungi; CAK43504; CAK43504; An01g01320.
DR   HOGENOM; HOG000161224; -.
DR   Proteomes; UP000006706; Chromosome 2R.
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   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;
DR   PRODOM; A2Q7N1.
DR   SWISS-2DPAGE; A2Q7N1.
KW   Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW   Glycosidase {ECO:0000256|RuleBase:RU361168, ECO:0000256|SAAS:SAAS01073727,
KW   ECO:0000313|EMBL:CAK43504.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361168, ECO:0000256|SAAS:SAAS01073724,
KW   ECO:0000313|EMBL:CAK43504.1}.
FT   DOMAIN          320..371
FT                   /note="Melibiase_C"
FT                   /evidence="ECO:0000259|Pfam:PF17801"
SQ   SEQUENCE   391 AA;  43330 MW;  255E0DFB14300919 CRC64;
     MMKRKSQLSS FTLVTAAILP FAHFVMGGTS LAQKPQMGWN SWNAFKATVN YTIVQEVISL
     FDTLGLKEAG YEYVLLDDGW ASYNRTSDGY LQANATSFPQ GIKALAQEVH GKGLKLGLYG
     DSGHYTCAWR PGSWGYEERD AQTFAGWGVD YLKYDNCGGF QSMTEAPQIR FGAMKNALTL
     SGRDIFYSVC GWGYQFPWHW GGDIGHSYRM SGDITTSFTN ETECQCKTAY CLNTGQYQTP
     GHWLDMDMLE VGNANFTLNQ QQTHFAFWAA LKSPLIIGAD LSKLSNDSLA VLTNKAIISI
     NQDALGEPVT YREAHSKEGL FQVWAGKVED GYVVLLLNEK SYPQTVSLSF ASLGLGSPQK
     VTELWSGQTL QDLSMISANP QSRQIDILNI K
//

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