XYNA_NIACI
ID XYNA_NIACI Reviewed; 213 AA.
AC P09850;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
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 Flags: Precursor;
GN Name=xlnA;
OS Niallia circulans (Bacillus circulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3405767; DOI=10.1093/nar/16.14.7187;
RA Yang R.C.A., MacKenzie C.R., Narang S.A.;
RT "Nucleotide sequence of a Bacillus circulans xylanase gene.";
RL Nucleic Acids Res. 16:7187-7187(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MUTAGENESIS.
RX PubMed=8019418; DOI=10.1002/pro.5560030312;
RA Wakarchuk W.W., Campbell R.L., Sung W.L., Davoodi J., Yaguchi M.;
RT "Mutational and crystallographic analyses of the active site residues of
RT the Bacillus circulans xylanase.";
RL Protein Sci. 3:467-475(1994).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=8756457; DOI=10.1021/bi9613234;
RA McIntosh L.P., Hand G., Johnson P.E., Joshi M.D., Koerner M.,
RA Plesniak L.A., Ziser L., Wakarchuk W.W., Withers S.G.;
RT "The pKa of the general acid/base carboxyl group of a glycosidase cycles
RT during catalysis: a 13C-NMR study of Bacillus circulans xylanase.";
RL Biochemistry 35:9958-9966(1996).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; X07723; CAA30553.1; -; Genomic_DNA.
DR PIR; S01734; S01734.
DR PDB; 1BCX; X-ray; 1.81 A; A=29-213.
DR PDB; 1BVV; X-ray; 1.80 A; A=29-213.
DR PDB; 1C5H; X-ray; 1.55 A; A=29-213.
DR PDB; 1C5I; X-ray; 1.80 A; A=29-213.
DR PDB; 1HV0; X-ray; 1.60 A; A=29-213.
DR PDB; 1HV1; X-ray; 1.80 A; A=29-213.
DR PDB; 1XNB; X-ray; 1.49 A; A=29-213.
DR PDB; 1XNC; X-ray; 1.60 A; A=29-213.
DR PDB; 2BVV; X-ray; 1.50 A; A=29-213.
DR PDB; 3LB9; X-ray; 3.00 A; A/B/C=29-213.
DR PDB; 3VZJ; X-ray; 2.41 A; A/B/C/D=29-213.
DR PDB; 3VZK; X-ray; 1.55 A; A/B=29-213.
DR PDB; 3VZL; X-ray; 2.00 A; A/B/C/D=29-213.
DR PDB; 3VZM; X-ray; 1.86 A; A=29-213.
DR PDB; 3VZN; X-ray; 1.67 A; A/B=29-213.
DR PDB; 3VZO; X-ray; 1.73 A; A=29-213.
DR PDB; 7VUG; EM; 3.20 A; R=29-213.
DR PDB; 7VUH; EM; 3.22 A; R=29-213.
DR PDB; 7VUI; EM; 3.30 A; R=29-213.
DR PDB; 7VUJ; EM; 3.80 A; R=29-213.
DR PDBsum; 1BCX; -.
DR PDBsum; 1BVV; -.
DR PDBsum; 1C5H; -.
DR PDBsum; 1C5I; -.
DR PDBsum; 1HV0; -.
DR PDBsum; 1HV1; -.
DR PDBsum; 1XNB; -.
DR PDBsum; 1XNC; -.
DR PDBsum; 2BVV; -.
DR PDBsum; 3LB9; -.
DR PDBsum; 3VZJ; -.
DR PDBsum; 3VZK; -.
DR PDBsum; 3VZL; -.
DR PDBsum; 3VZM; -.
DR PDBsum; 3VZN; -.
DR PDBsum; 3VZO; -.
DR PDBsum; 7VUG; -.
DR PDBsum; 7VUH; -.
DR PDBsum; 7VUI; -.
DR PDBsum; 7VUJ; -.
DR AlphaFoldDB; P09850; -.
DR BMRB; P09850; -.
DR SMR; P09850; -.
DR DrugBank; DB03389; alpha-D-Xylopyranose.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_BACCI; -.
DR BRENDA; 3.2.1.8; 649.
DR SABIO-RK; P09850; -.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; P09850; -.
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 Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033119; GH11_AS_2.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS00777; GH11_2; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal; Xylan degradation.
FT SIGNAL 1..28
FT CHAIN 29..213
FT /note="Endo-1,4-beta-xylanase"
FT /evidence="ECO:0000269|PubMed:3405767"
FT /id="PRO_0000007996"
FT DOMAIN 29..213
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062,
FT ECO:0000269|PubMed:8019418"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063,
FT ECO:0000269|PubMed:8019418"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:3LB9"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 78..101
FT /evidence="ECO:0007829|PDB:1XNB"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 131..144
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 148..162
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1XNB"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 190..203
FT /evidence="ECO:0007829|PDB:1XNB"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:1XNB"
SQ SEQUENCE 213 AA; 23359 MW; 4BA0A35238CC0135 CRC64;
MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS GGNYSVNWSN
TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT RSPLIEYYVV DSWGTYRPTG
TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR TTFTQYWSVR QSKRPTGSNA TITFTNHVNA
WKSHGMNLGS NWAYQVMATE GYQSSGSSNV TVW
