XYN1_GEOSE
ID XYN1_GEOSE Reviewed; 407 AA.
AC P40943; Q09LX3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 111.
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;
DE Flags: Precursor;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=T-6 / NCIMB 40221;
RX PubMed=8031084; DOI=10.1128/aem.60.6.1889-1896.1994;
RA Gat O., Lapidot A., Alchanati I., Regueros C., Shoham Y.;
RT "Cloning and DNA sequence of the gene coding for Bacillus
RT stearothermophilus T-6 xylanase.";
RL Appl. Environ. Microbiol. 60:1889-1896(1994).
RN [2]
RP PROTEIN SEQUENCE OF 29-73.
RC STRAIN=T-6;
RX PubMed=8328796; DOI=10.1128/aem.59.6.1725-1730.1993;
RA Khasin A., Alchanati I., Shoham Y.;
RT "Purification and characterization of a thermostable xylanase from Bacillus
RT stearothermophilus T-6.";
RL Appl. Environ. Microbiol. 59:1725-1730(1993).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: By xylose.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI49951.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ868502; ABI49951.1; ALT_INIT; Genomic_DNA.
DR PIR; I40570; I40570.
DR PDB; 1HIZ; X-ray; 2.40 A; A=29-407.
DR PDB; 1R85; X-ray; 1.45 A; A=29-407.
DR PDB; 1R86; X-ray; 1.80 A; A=29-407.
DR PDB; 1R87; X-ray; 1.67 A; A=29-407.
DR PDB; 3MMD; X-ray; 1.70 A; A=29-407.
DR PDB; 4PRW; X-ray; 1.80 A; A=29-407.
DR PDB; 4PUD; X-ray; 2.01 A; A=37-407.
DR PDB; 4PUE; X-ray; 2.20 A; A=37-407.
DR PDBsum; 1HIZ; -.
DR PDBsum; 1R85; -.
DR PDBsum; 1R86; -.
DR PDBsum; 1R87; -.
DR PDBsum; 3MMD; -.
DR PDBsum; 4PRW; -.
DR PDBsum; 4PUD; -.
DR PDBsum; 4PUE; -.
DR AlphaFoldDB; P40943; -.
DR SMR; P40943; -.
DR DrugBank; DB03389; alpha-D-Xylopyranose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR SABIO-RK; P40943; -.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; P40943; -.
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; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:8328796"
FT CHAIN 29..407
FT /note="Endo-1,4-beta-xylanase"
FT /id="PRO_0000007968"
FT DOMAIN 42..406
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 293
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1HIZ"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:1R85"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1R87"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 150..175
FT /evidence="ECO:0007829|PDB:1R85"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1R87"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 314..333
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:1R85"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:1R85"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:1R85"
SQ SEQUENCE 407 AA; 46763 MW; AD385C90B252B82A CRC64;
MRNVVRKPLT IGLALTLLLP MGMTATSAKN ADSYAKKPHI SALNAPQLDQ RYKNEFTIGA
AVEPYQLQNE KDVQMLKRHF NSIVAENVMK PISIQPEEGK FNFEQADRIV KFAKANGMDI
RFHTLVWHSQ VPQWFFLDKE GKPMVNETDP VKREQNKQLL LKRLETHIKT IVERYKDDIK
YWDVVNEVVG DDGKLRNSPW YQIAGIDYIK VAFQAARKYG GDNIKLYMND YNTEVEPKRT
ALYNLVKQLK EEGVPIDGIG HQSHIQIGWP SEAEIEKTIN MFAALGLDNQ ITELDVSMYG
WPPRAYPTYD AIPKQKFLDQ AARYDRLFKL YEKLSDKISN VTFWGIADNH TWLDSRADVY
YDANGNVVVD PNAPYAKVEK GKGKDAPFVF GPDYKVKPAY WAIIDHK
