(data stored in SCRATCH zone)

SWISSPROT: Q4WCV4_ASPFU

ID   Q4WCV4_ASPFU            Unreviewed;       512 AA.
AC   Q4WCV4;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 84.
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=AFUA_6G02560 {ECO:0000313|EMBL:EAL85784.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85784.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85784.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL85784.1}.
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DR   EMBL; AAHF01000012; EAL85784.1; -; Genomic_DNA.
DR   RefSeq; XP_747822.1; XM_742729.1.
DR   STRING; 746128.CADAFUBP00009306; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   EnsemblFungi; EAL85784; EAL85784; AFUA_6G02560.
DR   GeneID; 3505099; -.
DR   KEGG; afm:AFUA_6G02560; -.
DR   EuPathDB; FungiDB:Afu6g02560; -.
DR   HOGENOM; HOG000161224; -.
DR   InParanoid; Q4WCV4; -.
DR   KO; K07407; -.
DR   OMA; CEWGQEN; -.
DR   OrthoDB; 964130at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IBA:GO_Central.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR   GO; GO:0046477; P:glycosylceramide catabolic process; IBA:GO_Central.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
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; IPR000111; Glyco_hydro_27/36_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR006215; Glyco_hydro_melibiase.
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   PRINTS; PR00748; MELIBIASE.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WCV4.
DR   SWISS-2DPAGE; Q4WCV4.
KW   Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW   Glycosidase {ECO:0000256|RuleBase:RU361168, ECO:0000256|SAAS:SAAS01073727};
KW   Hydrolase {ECO:0000256|RuleBase:RU361168, ECO:0000256|SAAS:SAAS01073724};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN          371..435
FT                   /note="Melibiase_C"
FT                   /evidence="ECO:0000259|Pfam:PF17801"
SQ   SEQUENCE   512 AA;  56326 MW;  1DF138AABC656001 CRC64;
     MHISGYKIPS NQGQAIWRNI YCNCQLLLLW LRVTVFLQTL SSLHNGALFT AALRGALRPQ
     GFCIEQWLSS NTADGMVILD AAERIVSLGF KDLGYEYVVL DDCWSAGRNS SGYLIADSEK
     FPNGIAHLAD KVHELGLKIG IYSSAGRWTC ARYEGSLGYE EKDAALWASW GIDYLKYDNC
     YNEGEEGTPK LSFDRYNAMF KALNATGRPM LYSLCNWGVD GPWNFAPTIA NSWRTTGDLS
     NVWDRDDVNC PCSELDGLDC KTPGYKCSIM NVLNKAVYYP SKAIPGAWND LDMLQVGNGG
     LTDDESIAHM SLWAALKSPL LMTNVMTKID PPTLSILQNP AVLAVSQDPL ASTPVRQWRY
     FVDDVDENGK GEIQMYSGPL SGGDQLVLLL NAGSKAREMN ATLVDIFWES GAKGTAKQVK
     QHWDVYDLWA NRMSNEDAAA IINGTFTGPS PYNLTAMGGA HEVYSRPLPS NSKVLMGSKV
     GSVQPSGTVT AYVRPHGVAM LRLRATDKKD EL
//

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