XYNA_STRSQ
ID XYNA_STRSQ Reviewed; 464 AA.
AC B4XVN1;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Endo-1,4-beta-xylanase A;
DE Short=Xylanase A;
DE EC=3.2.1.8;
DE Flags: Precursor;
GN Name=xynAS9;
OS Streptomyces sp.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1931;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A XYLANASE, LACK OF
RP COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=S9;
RX PubMed=18521591; DOI=10.1007/s00253-008-1533-z;
RA Li N., Meng K., Wang Y., Shi P., Luo H., Bai Y., Yang P., Yao B.;
RT "Cloning, expression, and characterization of a new xylanase with broad
RT temperature adaptability from Streptomyces sp. S9.";
RL Appl. Microbiol. Biotechnol. 80:231-240(2008).
CC -!- FUNCTION: Contributes to hydrolysis of hemicellulose, the major
CC component of plant cell-walls. Hydrolyzes xylan to xylose and
CC xylobiose. {ECO:0000269|PubMed:18521591}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- COFACTOR:
CC Note=Does not require any standard metal (Mg(2+), Mn2(+), Ca(2+)).;
CC -!- ACTIVITY REGULATION: Completely inhibited by Hg(2+), unaffected by
CC EDTA. {ECO:0000269|PubMed:18521591}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=772.20 umol/min/mg enzyme for oat spelt xylan
CC {ECO:0000269|PubMed:18521591};
CC Vmax=490.87 umol/min/mg enzyme for birchwood xylan
CC {ECO:0000269|PubMed:18521591};
CC pH dependence:
CC Optimum pH is 6.5, more than 80% active between pH 5.0 and 7.0.
CC {ECO:0000269|PubMed:18521591};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius, more than 80% of activity
CC remains after 1 hour at 60 degrees Celsius.
CC {ECO:0000269|PubMed:18521591};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; EU153378; ABX71815.1; -; Genomic_DNA.
DR PDB; 3WUB; X-ray; 2.08 A; A=39-351.
DR PDB; 3WUE; X-ray; 2.15 A; A=39-351.
DR PDB; 3WUF; X-ray; 2.04 A; A=39-351.
DR PDB; 3WUG; X-ray; 1.88 A; A=39-351.
DR PDBsum; 3WUB; -.
DR PDBsum; 3WUE; -.
DR PDBsum; 3WUF; -.
DR PDBsum; 3WUG; -.
DR AlphaFoldDB; B4XVN1; -.
DR SMR; B4XVN1; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR BRENDA; 3.2.1.8; 11186.
DR UniPathway; UPA00114; -.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:UniProtKB.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal; Xylan degradation.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..464
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000424416"
FT DOMAIN 40..349
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT DOMAIN 354..457
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:3WUG"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:3WUG"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 200..210
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 216..231
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 266..279
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 282..301
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:3WUG"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:3WUG"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:3WUG"
SQ SEQUENCE 464 AA; 49868 MW; 4856950BC604B95C CRC64;
MFRHHPTRGR RTAGLLAAAL ATLSAGLTAV APAHPARADT ATLGELAEAK GRYFGSATDN
PELPDTQYTQ ILGSEFSQIT VGNTMKWQYT EPSRGRFDYT AAEEIVDLAE SNGQSVRGHT
LVWHNQLPSW VDDVPAGELL GVMRDHITHE VDHFKGRLIH WDVVNEAFEE DGSRRQSVFQ
QKIGDSYIAE AFKAARAADP DVKLYYNDYN IEGIGPKSDA VYEMVKSFKA QGIPIDGVGM
QAHLIAGQVP ASLQENIRRF ADLGVDVALT ELDIRMTLPR TAAKDAQQAT DYGAVVEACL
VVSRCVGITV WDYTDKYSWV PSVFPGQGAA LPWDEDFAKK PAYHAIAAAL NGGSPAPGGN
CTATYRVTSQ WQGGFTAEIT VGNDHTAPIT GWTVTWTLSS GQSISHMWNG NLTVNGQDVT
VRDVGYNGTL GGNGSTTFGF QGEGVADTPA DVTCTPGRPS GTSA
