AXE1_ASPOR
ID AXE1_ASPOR Reviewed; 307 AA.
AC Q75P26;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Acetylxylan esterase A;
DE EC=3.1.1.72;
DE Flags: Precursor;
GN Name=axeA; Synonyms=aceA, AoaxeA; ORFNames=AO090011000745;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX DOI=10.1016/j.jbiotec.2005.07.015;
RA Koseki T., Miwa Y., Akao T., Akita O., Hashizume K.;
RT "An Aspergillus oryzae acetyl xylan esterase: Molecular cloning and
RT characteristics of recombinant enzyme expressed in Pichia pastoris.";
RL J. Biotechnol. 121:381-389(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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. Displays the greatest hydrolytic
CC activity toward alpha-naphthylacetate (C2), lower activity toward
CC alpha-naphthylpropionate (C3) and no detectable activity toward acyl-
CC chain substrates containing four or more carbon atoms.
CC {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. The enzyme is stable between pH 6.0 and 7.0.
CC {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. Unstable at 40 degrees
CC Celsius with a half life of less than 60 min at 40 degrees Celsius
CC and 10 min at 50 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: The C-terminal carbohydrate-binding module (CBM) extension
CC found in soem acetylxylan esterases from other species is absent.
CC {ECO:0000305}.
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DR EMBL; AB167976; BAD12626.1; -; Genomic_DNA.
DR EMBL; AP007171; BAE65196.1; -; Genomic_DNA.
DR RefSeq; XP_001826329.1; XM_001826277.2.
DR AlphaFoldDB; Q75P26; -.
DR SMR; Q75P26; -.
DR CLAE; AXE1A_ASPOR; -.
DR ESTHER; aspor-axe1; Esterase_phb.
DR EnsemblFungi; BAE65196; BAE65196; AO090011000745.
DR GeneID; 5998432; -.
DR KEGG; aor:AO090011000745; -.
DR VEuPathDB; FungiDB:AO090011000745; -.
DR HOGENOM; CLU_027551_1_1_1; -.
DR OMA; IANMVKW; -.
DR BRENDA; 3.1.1.72; 522.
DR BRENDA; 3.1.1.73; 522.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000006564; Chromosome 7.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046555; F:acetylxylan esterase activity; IDA:AspGD.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IDA:AspGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR010126; Esterase_phb.
DR Pfam; PF10503; Esterase_PHB; 1.
DR SUPFAM; SSF53474; SSF53474; 2.
DR TIGRFAMs; TIGR01840; esterase_phb; 1.
PE 1: Evidence at protein level;
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..307
FT /note="Acetylxylan esterase A"
FT /id="PRO_0000393480"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 307 AA; 33286 MW; 7B08600B5BAC16D1 CRC64;
MILLSYLLTY LLCALTCSAR AIHNGRSLIP RAGSLEQVTD FGDNPSNVKM YIYVPTNLAS
NPGIIVAIHY CTGTAQAYYQ GSPYAQLAET HGFIVIYPES PYEGTCWDVS SQATLTHNGG
GNSNSIANMV TWTTKQYNAD SSKVFVTGTS SGAMMTNVMA ATYPNLFAAG VAYAGVPAGC
FLSTADQPDA WNSTCAQGQS ITTPEHWASI AEAMYPDYSG SRPKMQIYHG NVDTTLYPQN
YEETCKQWAG VFGYNYDAPE STESNTPEAN WSRTTWGPNL QGILAGGVGH NIQIHGDEDM
KWFGFTN
