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AGALG_ASPTN
ID   AGALG_ASPTN             Reviewed;         725 AA.
AC   Q0CEF5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Probable alpha-galactosidase G;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase G;
GN   Name=aglG; ORFNames=ATEG_07929;
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family. {ECO:0000305}.
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DR   EMBL; CH476604; EAU32191.1; -; Genomic_DNA.
DR   RefSeq; XP_001216550.1; XM_001216550.1.
DR   AlphaFoldDB; Q0CEF5; -.
DR   SMR; Q0CEF5; -.
DR   STRING; 341663.Q0CEF5; -.
DR   EnsemblFungi; EAU32191; EAU32191; ATEG_07929.
DR   GeneID; 4322588; -.
DR   VEuPathDB; FungiDB:ATEG_07929; -.
DR   eggNOG; ENOG502QWG1; Eukaryota.
DR   HOGENOM; CLU_009640_2_1_1; -.
DR   OMA; FNSWEAT; -.
DR   OrthoDB; 472260at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd14791; GH36; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 2.70.98.60; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR038417; Alpga-gal_N_sf.
DR   InterPro; IPR002252; Glyco_hydro_36.
DR   InterPro; IPR031705; Glyco_hydro_36_C.
DR   InterPro; IPR031704; Glyco_hydro_36_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF16874; Glyco_hydro_36C; 1.
DR   Pfam; PF16875; Glyco_hydro_36N; 1.
DR   PIRSF; PIRSF005536; Agal; 1.
DR   PRINTS; PR00743; GLHYDRLASE36.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; Magnesium;
KW   NAD; Polysaccharide degradation; Reference proteome; Secreted.
FT   CHAIN           1..725
FT                   /note="Probable alpha-galactosidase G"
FT                   /id="PRO_0000395068"
FT   ACT_SITE        484
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT   ACT_SITE        546
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        672
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   725 AA;  80322 MW;  FB549C2032C1F01F CRC64;
     MTIENGIAKA IYVDGTKFVL NGRHVSYCFH VDDETGDLRT DHFGGRVTGA IPVDPSPVVD
     GWTGMPDRVR REFPDQGRGD FRIPALRIRQ AEGHTVSALK YQSYTLLHGK PDLPGLPATF
     GTEKDVSTLV VHLRDEYSSV TADLIYSVFP EYNAIVRSVS ITNNGFQPIS IEALASFSTD
     LPYEDLEMIS LRGDWAREAH RMRRKVEYGT QGFGSTTGFS SHLHNPFLAL AHPSTTESQG
     EAWGFSLVYT GSFEVNVEKG SQGLTRAVLG FHPNQLSWPL SPGETLTSPE CVAVYSNHGL
     GGMSRSLHRL FRDHLIKSKF ATANRPVLLN SWEGLYFDID ETSMIRIAKE SAALGVKLLV
     MDDGWFGKDY PRTSDAAGLG DWVPNPARFP NGLAPMVDQI TSLKVANSSA NLLFGIWVEP
     EMVNPDSALY REHPEWALHA GSYPRTEQRN QLVLNLALLE VQEFIINFMT DLLSSAKISY
     VKWDLNRGIN ETSAPKATHA YMLGMYKVFD TLTSRFPDVL WEGCAAGGGR FDPGILQYFP
     QIWTSDDSDA VERIFIQMGS SLAYPASAMG AHISAVPNHQ TGRTTPLSLR AHVAMMGGSF
     GLELDPSQVS AEEKALIPEL IALAEKVNPI VLTGDMWRLS LPEESNWPAV QFISQDQSQV
     VLFYFQLSPN VNHSMPRVRL QGLDEDAMYR VDGAGPYSGA MLMNLGLQYS FRTEYGSRVV
     FLEKQ
 
 
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