AXE2_TALPU
ID AXE2_TALPU Reviewed; 234 AA.
AC O59893;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Acetylxylan esterase 2;
DE EC=3.1.1.72;
DE AltName: Full=AXE II;
DE Flags: Precursor;
GN Name=axe-2; Synonyms=axeII;
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 / MRNA], AND PROTEIN SEQUENCE OF 28-234.
RX PubMed=9506837; DOI=10.1016/s0014-5793(98)00055-6;
RA Gutierrez R., Cederlund E., Hjelmqvist L., Peirano A., Herrera F.,
RA Ghosh D., Duax W., Joernvall H., Eyzaguirre J.;
RT "Acetyl xylan esterase II from Penicillium purpurogenum is similar to an
RT esterase from Trichoderma reesei but lacks a cellulose binding domain.";
RL FEBS Lett. 423:35-38(1998).
RN [2]
RP PROTEIN SEQUENCE OF 28-57, 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).
RN [3]
RP INDUCTION.
RX PubMed=15174310; DOI=10.4067/s0716-97602004000100011;
RA Chavez R., Schachter K., Navarro C., Peirano A., Bull P., Eyzaguirre J.;
RT "The acetyl xylan esterase II gene from Penicillium purpurogenum is
RT differentially expressed in several carbon sources, and tightly regulated
RT by pH.";
RL Biol. Res. 37:107-113(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 28-234.
RX PubMed=10089308; DOI=10.1107/s0907444999000244;
RA Ghosh D., Erman M., Sawicki M., Lala P., Weeks D.R., Li N., Pangborn W.,
RA Thiel D.J., Joernvall H., Gutierrez R., Eyzaguirre J.;
RT "Determination of a protein structure by iodination: the structure of
RT iodinated acetylxylan esterase.";
RL Acta Crystallogr. D 55:779-784(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (0.9 ANGSTROMS) OF 28-234.
RX PubMed=11134051; DOI=10.1074/jbc.m008831200;
RA Ghosh D., Sawicki M., Lala P., Erman M., Pangborn W., Eyzaguirre J.,
RA Gutierrez R., Joernvall H., Thiel D.J.;
RT "Multiple conformations of catalytic serine and histidine in acetylxylan
RT esterase at 0.90 A.";
RL J. Biol. Chem. 276:11159-11166(2001).
CC -!- FUNCTION: Degrades acetylated xylans by cleaving acetyl side groups
CC from the hetero-xylan backbone. {ECO:0000269|PubMed:8756392}.
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. {ECO:0000269|PubMed:8756392};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:8756392};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8756392}.
CC -!- INDUCTION: Induced by xylan and repressed by glucose. Expressed at
CC neutral pH, but not under alkaline or acidic condtions.
CC {ECO:0000269|PubMed:15174310}.
CC -!- SIMILARITY: Belongs to the cutinase family. Acetylxylan esterase
CC subfamily. {ECO:0000305}.
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DR EMBL; AF015285; AAC39371.1; -; mRNA.
DR PDB; 1BS9; X-ray; 1.10 A; A=28-234.
DR PDB; 1G66; X-ray; 0.90 A; A=28-234.
DR PDB; 2AXE; X-ray; 1.80 A; A=28-234.
DR PDBsum; 1BS9; -.
DR PDBsum; 1G66; -.
DR PDBsum; 2AXE; -.
DR AlphaFoldDB; O59893; -.
DR SMR; O59893; -.
DR CLAE; AXE5B_PENPU; -.
DR ESTHER; penpu-axylest; Acetylxylan_esterase.
DR BioCyc; MetaCyc:MON-16378; -.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; O59893; -.
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; IPR000675; Cutinase/axe.
DR PANTHER; PTHR33630; PTHR33630; 1.
DR Pfam; PF01083; Cutinase; 1.
DR SMART; SM01110; Cutinase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Polysaccharide degradation;
KW Secreted; Serine esterase; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..27
FT /evidence="ECO:0000269|PubMed:8756392,
FT ECO:0000269|PubMed:9506837"
FT /id="PRO_0000234624"
FT CHAIN 28..234
FT /note="Acetylxylan esterase 2"
FT /id="PRO_0000234625"
FT ACT_SITE 117
FT /evidence="ECO:0000250"
FT ACT_SITE 202
FT /evidence="ECO:0000250"
FT ACT_SITE 214
FT /evidence="ECO:0000250"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..106
FT DISULFID 73..79
FT DISULFID 128..188
FT DISULFID 174..206
FT DISULFID 198..205
FT CONFLICT 57
FT /note="L -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:1G66"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1G66"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:1G66"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1G66"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1G66"
FT HELIX 84..105
FT /evidence="ECO:0007829|PDB:1G66"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1G66"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:1G66"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1G66"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:1G66"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:1G66"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1G66"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1G66"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1G66"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:1G66"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:1G66"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:1G66"
FT HELIX 217..233
FT /evidence="ECO:0007829|PDB:1G66"
SQ SEQUENCE 234 AA; 23478 MW; C033B3DA4E7BB6E1 CRC64;
MHSKFFAASL LGLGAAAIPL EGVMEKRSCP AIHVFGARET TASPGYGSSS TVVNGVLSAY
PGSTAEAINY PACGGQSSCG GASYSSSVAQ GIAAVASAVN SFNSQCPSTK IVLVGYSQGG
EIMDVALCGG GDPNQGYTNT AVQLSSSAVN MVKAAIFMGD PMFRAGLSYE VGTCAAGGFD
QRPAGFSCPS AAKIKSYCDA SDPYCCNGSN AATHQGYGSE YGSQALAFVK SKLG
