AXE1_TALPU
ID AXE1_TALPU Reviewed; 382 AA.
AC Q8NJP6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Acetylxylan esterase A;
DE EC=3.1.1.72;
DE AltName: Full=AXE I;
DE AltName: Full=Acetylxylan esterase 1;
DE Flags: Precursor;
GN Name=axeA; Synonyms=aceA, axe-1, axeI;
OS Talaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1266744;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-67; 215-220 AND
RP 227-248, GLYCOSYLATION, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=17008082; DOI=10.1016/j.mycres.2006.07.003;
RA Gordillo F., Caputo V., Peirano A., Chavez R., Van Beeumen J.,
RA Vandenberghe I., Claeyssens M., Bull P., Ravanal M.C., Eyzaguirre J.;
RT "Penicillium purpurogenum produces a family 1 acetyl xylan esterase
RT containing a carbohydrate-binding module: characterization of the protein
RT and its gene.";
RL Mycol. Res. 110:1129-1139(2006).
RN [2]
RP PROTEIN SEQUENCE OF 32-51, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8756392;
RA Egana L., Gutierrez R., Caputo V., Peirano A., Steiner J., Eyzaguirre J.;
RT "Purification and characterization of two acetyl xylan esterases from
RT Penicillium purpurogenum.";
RL Biotechnol. Appl. Biochem. 24:33-39(1996).
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:17008082,
CC ECO:0000269|PubMed:8756392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72;
CC -!- ACTIVITY REGULATION: Inactivated by phenylmethylsulfonylfluorid (PMSF),
CC a specific inhibitor of serine esterases.
CC {ECO:0000269|PubMed:17008082}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.3. {ECO:0000269|PubMed:8756392};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:8756392};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8756392}.
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 -!- PTM: Glycosylated. {ECO:0000269|PubMed:17008082}.
CC -!- MISCELLANEOUS: The promoter contains 1 xlnR-binding sequence (a
CC transcriptional activator in the absence of glucose), 5 creA-binding
CC sequences (a negatively acting regulatory protein mediating carbon
CC catabolyte repression), 1 pacC-binding sequence (a pH regulator), 3
CC alcR-binding sequences (an activator of alcohol and acetaldehyde
CC dehydrogenase genes) and 3 areA-binding sequences (a nitrogen
CC metabolism activator).
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA
CC subfamily. {ECO:0000305}.
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DR EMBL; AF529173; AAM93261.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NJP6; -.
DR SMR; Q8NJP6; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CLAE; AXE1B_PENPU; -.
DR ESTHER; penpu-AXEI; Esterase_phb.
DR BioCyc; MetaCyc:MON-16880; -.
DR BRENDA; 3.1.1.72; 4635.
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: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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Hydrolase; Polysaccharide degradation; Secreted;
KW Serine esterase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..31
FT /evidence="ECO:0000269|PubMed:17008082,
FT ECO:0000269|PubMed:8756392"
FT /id="PRO_0000234626"
FT CHAIN 32..382
FT /note="Acetylxylan esterase A"
FT /id="PRO_0000234627"
FT DOMAIN 346..382
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 35..307
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 308..345
FT /note="Ser/Thr-rich linker"
FT REGION 313..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 36
FT /note="S -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 40273 MW; 5AB9A7AF770B4410 CRC64;
MKSLSFSFLV TLFLYLTLSS ARTLGKDVNK RVTAGSLQQV TGFGDNASGT LMYIYVPKNL
ATNPGIVVAI HYCTGTAQAY YTGSPYAQLA EQYGFIVIYP QSPYSGTCWD VSSQAALTHN
GGGDSNSIAN MVTWTISQYN ANTAKVFVTG SSSGAMMTNV MAATYPELFA AATVYSGVGA
GCFYSSSNQA DAWNSSCATG SVISTPAVWG GIAKNMYSGY SGSRPRMQIY HGSADTTLYP
QNYYETCKQW AGVFGYNYDS PQSTLANTPD ANYQTTNWGP NLQGIYATGV GHTVPIHGAK
DMEWFGFSGS GSSSTTTASA TKTSTTSTTS TKTTSSTSST TTSSTGVAAH WGQCGGSGWT
GPTVCESGYT CTYSNAWYSQ CL
