ID   AXE1_TRIRE     STANDARD;      PRT;   302 AA.
AC   Q99034;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   07-FEB-2006, entry version 44.
DE   Acetylxylan esterase precursor (EC 3.1.1.72).
GN   Name=axe1;
OS   Trichoderma reesei (Hypocrea jecorina).
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 158-186, AND
RP   CHARACTERIZATION.
RC   STRAIN=QM9414 / Rut C-30;
RX   MEDLINE=96235218; PubMed=8647098;
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=QM9414 / Rut C-30;
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=QM9414 / Rut C-30;
RA   Sundberg M., Poutanen K.;
RT   "Purification and properties of two acetylxylan esterases of
RT   Trichoderma reesei.";
RL   Biotechnol. Appl. Biochem. 13:1-11(1991).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 32-238, AND MASS
RP   SPECTROMETRY.
RX   MEDLINE=98437545; PubMed=9761918; DOI=10.1107/S0907444997012213;
RA   Hakulinen N., Tenkanen M., Rouvinen J.;
RT   "Crystallization and preliminary X-ray diffraction studies of the
RT   catalytic 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
RT   esterase from Trichoderma reesei: insights into the deacetylation
RT   mechanism.";
RL   J. Struct. Biol. 132:180-190(2000).
CC   -!- FUNCTION: Degrades acetylated xylans by cleaving acetyl side
CC       groups from the hetero-xylan backbone.
CC   -!- CATALYTIC ACTIVITY: Deacetylation of xylans and xylo-
CC       oligosaccharides.
CC   -!- ENZYME REGULATION: Inhibited by phenylmethylsulfonyl flouride.
CC   -!- PATHWAY: Xylan degradation.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted protein.
CC   -!- PTM: Glycosylated.
CC   -!- SIMILARITY: Contains 1 CBM1 (fungal-type carbohydrate-binding)
CC       domain.
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DR   EMBL; Z69256; CAA93247.1; -; mRNA.
DR   PIR; S71334; S71334.
DR   PDB; 1QOZ; X-ray; A/B=32-238.
DR   InterPro; IPR000254; CBD_fun.
DR   InterPro; IPR000675; Cutinase.
DR   InterPro; IPR008262; Lipase_AS.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF01083; Cutinase; 1.
DR   ProDom; PD001821; CBD_fungal; 1.
DR   SMART; SM00236; fCBD; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS00120; LIPASE_SER; UNKNOWN_1.
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Polysaccharide degradation; Pyrrolidone carboxylic acid;
KW   Serine esterase; Signal.
FT   SIGNAL        1     20       Potential.
FT   PROPEP       21     31       Potential.
FT                                /FTId=PRO_0000020771.
FT   CHAIN        32    302       Acetylxylan esterase.
FT                                /FTId=PRO_0000020772.
FT   DOMAIN      266    302       CBM1.
FT   REGION      244    266       Linker (By similarity).
FT   ACT_SITE    121    121       By similarity.
FT   MOD_RES      32     32       Pyrrolidone carboxylic acid.
FT   CARBOHYD     94     94       N-linked (GlcNAc...) (Probable).
FT   DISULFID    274    291       By similarity.
FT   DISULFID    285    301       By similarity.
FT   STRAND       35     41
FT   TURN         44     45
FT   STRAND       48     49
FT   HELIX        51     63
FT   STRAND       64     64
FT   TURN         65     66
FT   STRAND       67     71
FT   STRAND       74     74
FT   STRAND       78     79
FT   HELIX        81     83
FT   TURN         84     85
FT   HELIX        88    109
FT   TURN        111    112
FT   STRAND      113    120
FT   TURN        121    121
FT   HELIX       122    132
FT   STRAND      134    134
FT   STRAND      136    136
FT   HELIX       137    139
FT   TURN        140    140
FT   STRAND      141    141
FT   STRAND      145    145
FT   STRAND      148    148
FT   HELIX       150    155
FT   STRAND      156    163
FT   TURN        165    166
FT   STRAND      168    168
FT   TURN        169    170
FT   TURN        172    173
FT   STRAND      174    177
FT   STRAND      180    181
FT   TURN        183    184
FT   TURN        188    189
FT   TURN        193    194
FT   HELIX       195    197
FT   STRAND      198    201
FT   TURN        204    205
FT   STRAND      207    211
FT   HELIX       215    219
FT   HELIX       221    236
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
//