XYNA_PENSI
ID XYNA_PENSI Reviewed; 302 AA.
AC P56588;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Endo-1,4-beta-xylanase;
DE Short=Xylanase;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase;
OS Penicillium simplicissimum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS),
RP AND PYROGLUTAMATE FORMATION AT GLN-1.
RC STRAIN=BT 2246;
RX PubMed=9792094; DOI=10.1002/pro.5560071004;
RA Schmidt A., Schlacher A., Steiner W., Schwab H., Kratky C.;
RT "Structure of the xylanase from Penicillium simplicissimum.";
RL Protein Sci. 7:2081-2088(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX PubMed=10029534; DOI=10.1021/bi982108l;
RA Schmidt A., Gubitz G.M., Kratky C.;
RT "Xylan binding subsite mapping in the xylanase from Penicillium
RT simplicissimum using xylooligosaccharides as cryo-protectant.";
RL Biochemistry 38:2403-2412(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; AF070417; AAC23574.1; -; Genomic_DNA.
DR PDB; 1B30; X-ray; 2.25 A; A=2-302.
DR PDB; 1B31; X-ray; 1.75 A; A=1-302.
DR PDB; 1B3V; X-ray; 2.40 A; A=1-302.
DR PDB; 1B3W; X-ray; 2.60 A; A=2-302.
DR PDB; 1B3X; X-ray; 2.20 A; A=2-302.
DR PDB; 1B3Y; X-ray; 2.45 A; A=2-302.
DR PDB; 1B3Z; X-ray; 2.30 A; A=2-302.
DR PDB; 1BG4; X-ray; 1.75 A; A=2-302.
DR PDBsum; 1B30; -.
DR PDBsum; 1B31; -.
DR PDBsum; 1B3V; -.
DR PDBsum; 1B3W; -.
DR PDBsum; 1B3X; -.
DR PDBsum; 1B3Y; -.
DR PDBsum; 1B3Z; -.
DR PDBsum; 1BG4; -.
DR AlphaFoldDB; P56588; -.
DR SMR; P56588; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR BioCyc; MetaCyc:MON-16225; -.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; P56588; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Disulfide bond; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Pyrrolidone carboxylic acid;
KW Secreted; Xylan degradation.
FT CHAIN 1..302
FT /note="Endo-1,4-beta-xylanase"
FT /id="PRO_0000184067"
FT DOMAIN 21..301
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 132
FT /note="Proton donor"
FT ACT_SITE 238
FT /note="Nucleophile"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9792094"
FT DISULFID 256..262
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:1B31"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1B3X"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:1B31"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 219..227
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1B31"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1B31"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:1B31"
SQ SEQUENCE 302 AA; 32551 MW; EE7821FA58687FFC CRC64;
QASVSIDAKF KAHGKKYLGT IGDQYTLTKN TKNPAIIKAD FGQLTPENSM KWDATEPNRG
QFTFSGSDYL VNFAQSNGKL IRGHTLVWHS QLPGWVSSIT DKNTLISVLK NHITTVMTRY
KGKIYAWDVL NEIFNEDGSL RNSVFYNVIG EDYVRIAFET ARSVDPNAKL YINDYNLDSA
GYSKVNGMVS HVKKWLAAGI PIDGIGSQTH LGAGAGSAVA GALNALASAG TKEIAITELD
IAGASSTDYV NVVNACLNQA KCVGITVWGV ADPDSWRSSS SPLLFDGNYN PKAAYNAIAN
AL
