AXE1_HYPJE
ID AXE1_HYPJE Reviewed; 302 AA.
AC Q99034;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Acetylxylan esterase;
DE EC=3.1.1.72;
DE Flags: Precursor;
GN Name=axe1;
OS Hypocrea jecorina (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 158-186, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 56765 / Rut C-30;
RX PubMed=8647098; DOI=10.1111/j.1432-1033.1996.0553p.x;
RA Margolles-Clark E., Tenkanen M., Soederlund H., Penttilae M.;
RT "Acetyl xylan esterase from Trichoderma reesei contains an active-site
RT serine residue and a cellulose-binding domain.";
RL Eur. J. Biochem. 237:553-560(1996).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 56765 / Rut C-30;
RX DOI=10.1007/BF00172542;
RA Poutanen K., Sundberg M., Korte H., Puls J.;
RT "Deacetylation of xylans by acetyl esterases of Trichoderma reesei.";
RL Appl. Microbiol. Biotechnol. 33:506-510(1990).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=ATCC 56765 / Rut C-30;
RA Sundberg M., Poutanen K.;
RT "Purification and properties of two acetylxylan esterases of Trichoderma
RT reesei.";
RL Biotechnol. Appl. Biochem. 13:1-11(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 32-238, PYROGLUTAMATE FORMATION AT
RP GLN-32, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=9761918; DOI=10.1107/s0907444997012213;
RA Hakulinen N., Tenkanen M., Rouvinen J.;
RT "Crystallization and preliminary X-ray diffraction studies of the catalytic
RT core of acetyl xylan esterase from Trichoderma reesei.";
RL Acta Crystallogr. D 54:430-432(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-238.
RX PubMed=11243887; DOI=10.1006/jsbi.2000.4318;
RA Hakulinen N., Tenkanen M., Rouvinen J.;
RT "Three-dimensional structure of the catalytic core of acetylxylan esterase
RT from Trichoderma reesei: insights into the deacetylation mechanism.";
RL J. Struct. Biol. 132:180-190(2000).
CC -!- FUNCTION: Degrades acetylated xylans by cleaving acetyl side groups
CC from the hetero-xylan backbone. {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72;
CC -!- ACTIVITY REGULATION: Inhibited by phenylmethylsulfonyl flouride.
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the cutinase family. Acetylxylan esterase
CC subfamily. {ECO:0000305}.
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DR EMBL; Z69256; CAA93247.1; -; mRNA.
DR PIR; S71334; S71334.
DR PDB; 1QOZ; X-ray; 1.90 A; A/B=33-238.
DR PDBsum; 1QOZ; -.
DR AlphaFoldDB; Q99034; -.
DR SMR; Q99034; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CLAE; AXE5A_TRIRE; -.
DR ESTHER; hypje-axylest; Acetylxylan_esterase.
DR KEGG; ag:CAA93247; -.
DR VEuPathDB; FungiDB:TrQ_007363; -.
DR OMA; ADPFCCN; -.
DR BioCyc; MetaCyc:MON-16372; -.
DR BRENDA; 3.1.1.72; 6451.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; Q99034; -.
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; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR000675; Cutinase/axe.
DR PANTHER; PTHR33630; PTHR33630; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01083; Cutinase; 1.
DR SMART; SM01110; Cutinase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00120; LIPASE_SER; 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 Pyrrolidone carboxylic acid; Secreted; Serine esterase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..31
FT /evidence="ECO:0000255"
FT /id="PRO_0000020771"
FT CHAIN 32..302
FT /note="Acetylxylan esterase"
FT /id="PRO_0000020772"
FT DOMAIN 266..302
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 236..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..266
FT /note="Linker"
FT /evidence="ECO:0000250"
FT ACT_SITE 121
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9761918"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 274..291
FT /evidence="ECO:0000250"
FT DISULFID 285..301
FT /evidence="ECO:0000250"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1QOZ"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1QOZ"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:1QOZ"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1QOZ"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1QOZ"
FT HELIX 88..109
FT /evidence="ECO:0007829|PDB:1QOZ"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1QOZ"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:1QOZ"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1QOZ"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:1QOZ"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:1QOZ"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1QOZ"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1QOZ"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1QOZ"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:1QOZ"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:1QOZ"
FT HELIX 221..236
FT /evidence="ECO:0007829|PDB:1QOZ"
SQ SEQUENCE 302 AA; 30754 MW; BB6EDCA2971A9F2A CRC64;
MPSVKETLTL LLSQAFLATG SPVDGETVVK RQCPAIHVFG ARETTVSQGY GSSATVVNLV
IQAHPGTTSE AIVYPACGGQ ASCGGISYAN SVVNGTNAAA AAINNFHNSC PDTQLVLVGY
SQGAQIFDNA LCGGGDPGEG ITNTAVPLTA GAVSAVKAAI FMGDPRNIHG LPYNVGTCTT
QGFDARPAGF VCPSASKIKS YCDAADPYCC TGNDPNVHQG YGQEYGQQAL AFINSQLSSG
GSQPPGGGPT STSRPTSTRT GSSPGPTQTH WGQCGGQGWT GPTQCESGTT CQVISQWYSQ
CL
