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EXGA_ASPFU
ID   EXGA_ASPFU              Reviewed;         416 AA.
AC   Q4WK60;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Probable glucan 1,3-beta-glucosidase A;
DE            EC=3.2.1.58;
DE   AltName: Full=Exo-1,3-beta-glucanase 1;
DE   AltName: Full=Exo-1,3-beta-glucanase A;
DE   Flags: Precursor;
GN   Name=exgA; Synonyms=exg1; ORFNames=AFUA_1G03600;
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;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
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.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC       the main structural component of the cell wall. It could also function
CC       biosynthetically as a transglycosylase (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC         reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC         EC=3.2.1.58;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AAHF01000007; EAL88072.1; -; Genomic_DNA.
DR   RefSeq; XP_750110.1; XM_745017.1.
DR   AlphaFoldDB; Q4WK60; -.
DR   SMR; Q4WK60; -.
DR   STRING; 746128.CADAFUBP00000394; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EnsemblFungi; EAL88072; EAL88072; AFUA_1G03600.
DR   GeneID; 3507984; -.
DR   KEGG; afm:AFUA_1G03600; -.
DR   VEuPathDB; FungiDB:Afu1g03600; -.
DR   eggNOG; ENOG502QPYU; Eukaryota.
DR   HOGENOM; CLU_004624_0_1_1; -.
DR   InParanoid; Q4WK60; -.
DR   OMA; DTHHYQV; -.
DR   OrthoDB; 896412at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:1990819; C:actin fusion focus; IEA:EnsemblFungi.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0000935; C:division septum; IEA:EnsemblFungi.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IEA:EnsemblFungi.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006073; P:cellular glucan metabolic process; IBA:GO_Central.
DR   GO; GO:0070879; P:fungal-type cell wall beta-glucan metabolic process; IEA:EnsemblFungi.
DR   GO; GO:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Manganese; Metal-binding;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..416
FT                   /note="Probable glucan 1,3-beta-glucosidase A"
FT                   /id="PRO_0000393530"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        308
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        291..415
FT                   /evidence="ECO:0000250"
FT   DISULFID        316..342
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  45687 MW;  E415DC7AD94260C6 CRC64;
     MIFKFSQKAL VALYLVVGLA EAVPSKSRVV SRASTFDYNG IVRGVNIGGW LVLEPWITPS
     IFDNAGDAAV DEWTLTATLG QDQAKAVLSQ HWSTFITQDD FQQIAQAGMN HVRIPIGYWA
     VSSLPDEPYV DGQLEYLDNA ISWAREAGLK VVIDLHGAPG SQNGFDNSGR KGPIAWQQGD
     TVSQTVDAFR ALAERYLPQS DVVTAIEALN EPNIPGGVSE AGLRDYYNQI ADVVRQIDPG
     TSVFLSDGFL STESWNGFKT GEDVVMDTHH YEMFDNYLIS LDIDGHVKSA CDFGKQIEGS
     DKPVVVGEWS GAVTDCTKHL NGKGVSTRYQ GEYANNVKYG DCANTTQGSV ADLSDQERTD
     TRRFIEAQLD AYEGKNGWLF WTWKTEGAPG WDMQDLLANG VFPSPLTDRQ FPNQCA
 
 
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