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AXE1_ASPFU
ID   AXE1_ASPFU              Reviewed;         371 AA.
AC   Q4WBW4;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Probable acetylxylan esterase A;
DE            EC=3.1.1.72;
DE   Flags: Precursor;
GN   Name=axeA; Synonyms=aceA; ORFNames=AFUA_8G06570;
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: Acetylxylan esterase involved in the hydrolysis of xylan, a
CC       major structural heterogeneous polysaccharide found in plant biomass
CC       representing the second most abundant polysaccharide in the biosphere,
CC       after cellulose. Degrades acetylated xylans by cleaving acetyl side
CC       groups from the hetero-xylan backbone (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC         EC=3.1.1.72;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: Has a modular structure: a carbohydrate esterase catalytic
CC       module at the N-terminus, a linker rich in serines and threonines, and
CC       a C-terminal carbohydrate-binding module (CBM). The genes for catalytic
CC       modules and CBMs seem to have evolved separately and have been linked
CC       by gene fusion.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAHF01000013; EAL85420.1; -; Genomic_DNA.
DR   RefSeq; XP_747458.1; XM_742365.1.
DR   AlphaFoldDB; Q4WBW4; -.
DR   SMR; Q4WBW4; -.
DR   STRING; 746128.CADAFUBP00007907; -.
DR   ESTHER; aspfu-axe1; Esterase_phb.
DR   EnsemblFungi; EAL85420; EAL85420; AFUA_8G06570.
DR   GeneID; 3504738; -.
DR   KEGG; afm:AFUA_8G06570; -.
DR   VEuPathDB; FungiDB:Afu8g06570; -.
DR   eggNOG; ENOG502QTDU; Eukaryota.
DR   HOGENOM; CLU_027551_1_1_1; -.
DR   InParanoid; Q4WBW4; -.
DR   OMA; IANMVKW; -.
DR   OrthoDB; 1169544at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000002530; Chromosome 8.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR010126; Esterase_phb.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF10503; Esterase_PHB; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF53474; SSF53474; 2.
DR   TIGRFAMs; TIGR01840; esterase_phb; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Serine esterase;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..371
FT                   /note="Probable acetylxylan esterase A"
FT                   /id="PRO_0000393479"
FT   DOMAIN          335..371
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          32..304
FT                   /note="Catalytic"
FT   REGION          305..336
FT                   /note="Ser/Thr-rich linker"
FT   REGION          305..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   371 AA;  39252 MW;  66AA089FB0675CC9 CRC64;
     MRALSVFVAL FSFLALSSAS PGQDVAKRVT SGSLQQVTNF GSNPSGTLMY IYVPNNLATK
     PGIVVAIHYC TGTAQAYYTG SPYAQLAEKY GFIVIYPQSP YSGTCWDVSS QSALTHNGGG
     DSNSIANMVT WTISQYNADT SKVFVTGSSS GAMMTNVMAA TYPELFAAAT VYSGVPAGCF
     YSSSNQVNGW NSSCAQGNVI STPEVWGGIA KAMYPGYTGP RPRMQIYHGS VDTTLYPQNY
     YETCKQWAGV FGYNYNSPQS TQSNTPQANY QTTIWGPNLQ GIFATGVGHT VPIHGEQDME
     WFGFTGGSSS TTTTATTPPT TSTTTSSGGS STSTGVAEHW GQCGGNGWTG PTACASGYTC
     TVINEWYSQC L
 
 
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