AXE1_ASPAW
ID AXE1_ASPAW Reviewed; 304 AA.
AC Q92194;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Acetylxylan esterase A;
DE EC=3.1.1.72;
DE Flags: Precursor;
GN Name=axeA; Synonyms=aceA;
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-48; 245-254;
RP 260-279 AND 298-304, FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=9291122; DOI=10.1042/bj3260485;
RA Koseki T., Furuse S., Iwano K., Sakai H., Matsuzawa H.;
RT "An Aspergillus awamori acetylesterase: purification of the enzyme, and
RT cloning and sequencing of the gene.";
RL Biochem. J. 326:485-490(1997).
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. {ECO:0000269|PubMed:9291122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72;
CC -!- ACTIVITY REGULATION: Inactivated by di-isopropylfluorophosphate and
CC phenylmethylsulfonylfluorid (PMSF), a specific inhibitor of serine
CC esterases. {ECO:0000269|PubMed:9291122}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. Activity is significantly retained from pH 6.0 to
CC 9.0. {ECO:0000269|PubMed:9291122};
CC Temperature dependence:
CC Activity is decreased at temperatures higher than 40 degrees Celsius.
CC {ECO:0000269|PubMed:9291122};
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 some acetylxylan esterases from other species is absent.
CC {ECO:0000305}.
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DR EMBL; D87681; BAA13434.2; -; Genomic_DNA.
DR PDB; 5X6S; X-ray; 1.90 A; A/B=30-304.
DR PDBsum; 5X6S; -.
DR AlphaFoldDB; Q92194; -.
DR SMR; Q92194; -.
DR ESTHER; aspaw-AXE1; Esterase_phb.
DR UniPathway; UPA00114; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
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; 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 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycoprotein; Hydrolase;
KW Polysaccharide degradation; Secreted; Serine esterase; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..304
FT /note="Acetylxylan esterase A"
FT /id="PRO_0000393474"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5X6S"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:5X6S"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:5X6S"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:5X6S"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:5X6S"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:5X6S"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:5X6S"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:5X6S"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:5X6S"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:5X6S"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:5X6S"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:5X6S"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:5X6S"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:5X6S"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:5X6S"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:5X6S"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:5X6S"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:5X6S"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:5X6S"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:5X6S"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:5X6S"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:5X6S"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:5X6S"
SQ SEQUENCE 304 AA; 32729 MW; 73068FB386400B6E CRC64;
MLLSTHLLFV ITTLVTSLLH PIDGHAVKRS GSLQQVTDFG DNPTNVGMYI YVPNNLASNP
GIVVAIHYCT GTGPGYYGDS PYATLSEQYG FIVIYPSSPY SGGCWDVSSQ ATLTHNGGGN
SNSIANMVTW TISKYGADSS KVFVTGSSSG AMMTNVMAAT YPELFAAATV YSGVSAGCFY
SNTNQVDGWN STCAQGDVIT TPEHWASIAE AMYSGYSGSR PRMQIYHGSI DTTLYPQNYY
ETCKQWAGVF GYDYSAPEKT EANTPQTNYE TTIWGDSLQG IFATGVGHTV PIHGDKDMEW
FGFA
