XYNA_THEAU
ID XYNA_THEAU Reviewed; 329 AA.
AC P23360; Q9UQZ4;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 4.
DT 25-MAY-2022, entry version 118.
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 AltName: Full=TAXI;
DE Flags: Precursor;
GN Name=XYNA;
OS Thermoascus aurantiacus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Thermoascus.
OX NCBI_TaxID=5087;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bousson J.-C., Parriche M.;
RT "Cloning, sequencing and overexpression of Thermoascus aurantiacus xylanase
RT A (xynA).";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 27-328.
RA Srinivasa B.R., Vithayathil P.J., Roy R.P., Swaminathan K.R.;
RT "Significance of structural homology of Thermoascus aurantiacus xylanase
RT with the exoglucanase of Cellulomonas fimi.";
RL J. Protein Chem. 9:337-338(1990).
RN [3]
RP PROTEIN SEQUENCE OF 27-328.
RX PubMed=1924265;
RA Srinivasa B.R., Swaminathan K.R., Ganapathy C., Roy R.P., Murthy S.K.,
RA Vithayathil P.J.;
RT "The primary structure of xylanase from Thermoascus aurantiacus.";
RL Protein Seq. Data Anal. 4:15-20(1991).
RN [4]
RP PROTEIN SEQUENCE OF 27-328, AND X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS).
RC STRAIN=IMI 216529;
RX PubMed=11223515; DOI=10.1107/s0907444900019089;
RA Teixeira S., Lo Leggio L., Pickersgill R.W., Cardin C.;
RT "Anisotropic refinement of the structure of Thermoascus aurantiacus
RT xylanase I.";
RL Acta Crystallogr. D 57:385-392(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS).
RC STRAIN=IMI 216529;
RX PubMed=10409823;
RX DOI=10.1002/(sici)1097-0134(19990815)36:3<295::aid-prot4>3.0.co;2-6;
RA Lo Leggio L., Kalogiannis S., Bhat M.K., Pickersgill R.W.;
RT "High resolution structure and sequence of T. aurantiacus xylanase I:
RT implications for the evolution of thermostability in family 10 xylanases
RT and enzymes with (beta)alpha-barrel architecture.";
RL Proteins 36:295-306(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
CC -!- CAUTION: Ref.2, PubMed:1924265 and PubMed:10409823 N-terminal
CC modification was incorrect. X-ray structure has cyclic pyroglutamic
CC acid. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.2; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=Ref.3; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AJ132635; CAB65468.1; -; Genomic_DNA.
DR EMBL; AF127529; AAF24127.1; -; Genomic_DNA.
DR PIR; A59381; A59381.
DR PDB; 1GOK; X-ray; 1.14 A; A=28-329.
DR PDB; 1GOM; X-ray; 1.92 A; A=28-329.
DR PDB; 1GOO; X-ray; 1.87 A; A=28-329.
DR PDB; 1GOQ; X-ray; 1.80 A; A=28-329.
DR PDB; 1GOR; X-ray; 1.70 A; A=28-329.
DR PDB; 1I1W; X-ray; 0.89 A; A=28-329.
DR PDB; 1I1X; X-ray; 1.11 A; A=27-329.
DR PDB; 1K6A; X-ray; 1.14 A; A=27-329.
DR PDB; 1TUX; X-ray; 1.80 A; A=28-325.
DR PDB; 2BNJ; X-ray; 1.60 A; A=28-329.
DR PDB; 3NYD; X-ray; 1.23 A; A/B=27-329.
DR PDB; 3O2L; X-ray; 2.00 A; A=27-329.
DR PDB; 4BS0; X-ray; 1.09 A; A/B=28-329.
DR PDB; 5RG4; X-ray; 1.99 A; A/B=28-329.
DR PDB; 5RG5; X-ray; 1.62 A; A/B=28-329.
DR PDB; 5RG6; X-ray; 1.35 A; A/B=28-329.
DR PDB; 5RG7; X-ray; 1.47 A; A/B=28-329.
DR PDB; 5RG8; X-ray; 1.73 A; A=27-329.
DR PDB; 5RG9; X-ray; 1.47 A; A/B=28-329.
DR PDB; 5RGA; X-ray; 1.86 A; A/B=28-329.
DR PDB; 5RGB; X-ray; 1.42 A; A/B=28-329.
DR PDB; 5RGC; X-ray; 1.39 A; A/B=28-329.
DR PDB; 5RGD; X-ray; 1.60 A; A/B=28-329.
DR PDB; 5RGE; X-ray; 1.77 A; A=28-329.
DR PDB; 5RGF; X-ray; 1.46 A; A/B=28-329.
DR PDB; 7K4P; X-ray; 1.08 A; A/B=28-329.
DR PDB; 7K4Q; X-ray; 1.28 A; A/B=28-329.
DR PDB; 7K4R; X-ray; 1.57 A; A=28-329.
DR PDB; 7K4S; X-ray; 2.00 A; A=28-329.
DR PDB; 7K4T; X-ray; 1.00 A; A=28-329.
DR PDB; 7K4U; X-ray; 1.30 A; A=28-328.
DR PDB; 7K4V; X-ray; 1.30 A; A=28-329.
DR PDB; 7K4W; X-ray; 1.90 A; A=28-329.
DR PDB; 7K4X; X-ray; 1.60 A; A/B=28-329.
DR PDB; 7K4Y; X-ray; 1.80 A; A=28-329.
DR PDB; 7K4Z; X-ray; 1.08 A; A=28-329.
DR PDBsum; 1GOK; -.
DR PDBsum; 1GOM; -.
DR PDBsum; 1GOO; -.
DR PDBsum; 1GOQ; -.
DR PDBsum; 1GOR; -.
DR PDBsum; 1I1W; -.
DR PDBsum; 1I1X; -.
DR PDBsum; 1K6A; -.
DR PDBsum; 1TUX; -.
DR PDBsum; 2BNJ; -.
DR PDBsum; 3NYD; -.
DR PDBsum; 3O2L; -.
DR PDBsum; 4BS0; -.
DR PDBsum; 5RG4; -.
DR PDBsum; 5RG5; -.
DR PDBsum; 5RG6; -.
DR PDBsum; 5RG7; -.
DR PDBsum; 5RG8; -.
DR PDBsum; 5RG9; -.
DR PDBsum; 5RGA; -.
DR PDBsum; 5RGB; -.
DR PDBsum; 5RGC; -.
DR PDBsum; 5RGD; -.
DR PDBsum; 5RGE; -.
DR PDBsum; 5RGF; -.
DR PDBsum; 7K4P; -.
DR PDBsum; 7K4Q; -.
DR PDBsum; 7K4R; -.
DR PDBsum; 7K4S; -.
DR PDBsum; 7K4T; -.
DR PDBsum; 7K4U; -.
DR PDBsum; 7K4V; -.
DR PDBsum; 7K4W; -.
DR PDBsum; 7K4X; -.
DR PDBsum; 7K4Y; -.
DR PDBsum; 7K4Z; -.
DR AlphaFoldDB; P23360; -.
DR SMR; P23360; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR CLAE; XYN10A_THEAU; -.
DR BRENDA; 3.2.1.8; 6294.
DR EvolutionaryTrace; P23360; -.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
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 Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Pyrrolidone carboxylic acid; Signal; Xylan degradation.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:11223515,
FT ECO:0000269|PubMed:1924265, ECO:0000269|Ref.2"
FT CHAIN 27..329
FT /note="Endo-1,4-beta-xylanase"
FT /id="PRO_0000007985"
FT DOMAIN 29..326
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 157
FT /note="Proton donor"
FT ACT_SITE 263
FT /note="Nucleophile"
FT MOD_RES 27
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P56588"
FT DISULFID 281..287
FT CONFLICT 243
FT /note="G -> S (in Ref. 1; CAB65468/AAF24127)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="P -> S (in Ref. 1; CAB65468/AAF24127)"
FT /evidence="ECO:0000305"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:7K4P"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:1I1W"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7K4P"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 127..144
FT /evidence="ECO:0007829|PDB:1I1W"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1I1W"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:7K4U"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1I1W"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1I1W"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:1I1W"
SQ SEQUENCE 329 AA; 35686 MW; 8FE2F3D1A9F89815 CRC64;
MVRPTILLTS LLLAPFAAAS PILEERQAAQ SVDQLIKARG KVYFGVATDQ NRLTTGKNAA
IIQADFGQVT PENSMKWDAT EPSQGNFNFA GADYLVNWAQ QNGKLIRGHT LVWHSQLPSW
VSSITDKNTL TNVMKNHITT LMTRYKGKIR AWDVVNEAFN EDGSLRQTVF LNVIGEDYIP
IAFQTARAAD PNAKLYINDY NLDSASYPKT QAIVNRVKQW RAAGVPIDGI GSQTHLSAGQ
GAGVLQALPL LASAGTPEVA ITELDVAGAS PTDYVNVVNA CLNVQSCVGI TVWGVADPDS
WRASTTPLLF DGNFNPKPAY NAIVQDLQQ
