ID XYNA_STRLI Reviewed; 477 AA. AC P26514; P96464; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 28-JUN-2023, entry version 129. DE RecName: Full=Endo-1,4-beta-xylanase A; DE Short=Xylanase A; DE EC=3.2.1.8; DE AltName: Full=1,4-beta-D-xylan xylanohydrolase A; DE Flags: Precursor; GN Name=xlnA; OS Streptomyces lividans. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1916; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 42-92. RC STRAIN=66 / 1326; RX PubMed=1743521; DOI=10.1016/0378-1119(91)90299-q; RA Shareck F., Roy C., Yaguchi M., Morosoli R., Kluepfel D.; RT "Sequences of three genes specifying xylanases in Streptomyces lividans."; RL Gene 107:75-82(1991). RN [2] RP SEQUENCE REVISION TO 20 AND 140-141. RA Shareck F.; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 42-340. RX PubMed=8063693; DOI=10.1016/s0021-9258(17)31892-6; RA Derewenda U., Swenson L., Green R., Wei Y.Y., Morosoli R., Shareck F., RA Kluepfel D., Derewenda Z.S.; RT "Crystal structure, at 2.6-A resolution, of the Streptomyces lividans RT xylanase A, a member of the F family of beta-1,4-D-glycanases."; RL J. Biol. Chem. 269:20811-20814(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 348-477, AND DISULFIDE BONDS. RX PubMed=11914070; DOI=10.1021/bi015865j; RA Notenboom V., Boraston A.B., Williams S.J., Kilburn D.G., Rose D.R.; RT "High-resolution crystal structures of the lectin-like xylan binding domain RT from Streptomyces lividans xylanase 10A with bound substrates reveal a RT novel mode of xylan binding."; RL Biochemistry 41:4246-4254(2002). CC -!- FUNCTION: Contributes to hydrolyze hemicellulose, the major component CC of plant cell-walls. XLNA and XLNB seem to act sequentially on the CC substrate to yield xylobiose and xylose as carbon sources. 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M64551; AAC26525.1; -; Genomic_DNA. DR PIR; JS0589; JS0589. DR PDB; 1E0V; X-ray; 1.70 A; A=42-343. DR PDB; 1E0W; X-ray; 1.20 A; A=42-343. DR PDB; 1E0X; X-ray; 1.65 A; A/B=42-350. DR PDB; 1KNL; X-ray; 1.20 A; A=348-477. DR PDB; 1KNM; X-ray; 1.20 A; A=348-477. DR PDB; 1MC9; X-ray; 1.70 A; A=348-477. DR PDB; 1OD8; X-ray; 1.05 A; A=42-354. DR PDB; 1V0K; X-ray; 1.03 A; A=42-354. DR PDB; 1V0L; X-ray; 0.98 A; A=42-354. DR PDB; 1V0M; X-ray; 1.07 A; A=42-354. DR PDB; 1V0N; X-ray; 1.10 A; A=42-354. DR PDB; 1XAS; X-ray; 2.60 A; A=42-340. DR PDBsum; 1E0V; -. DR PDBsum; 1E0W; -. DR PDBsum; 1E0X; -. DR PDBsum; 1KNL; -. DR PDBsum; 1KNM; -. DR PDBsum; 1MC9; -. DR PDBsum; 1OD8; -. DR PDBsum; 1V0K; -. DR PDBsum; 1V0L; -. DR PDBsum; 1V0M; -. DR PDBsum; 1V0N; -. DR PDBsum; 1XAS; -. DR AlphaFoldDB; P26514; -. DR BMRB; P26514; -. DR SMR; P26514; -. DR DrugBank; DB03389; alpha-D-Xylopyranose. DR DrugBank; DB03366; Imidazole. DR DrugBank; DB04465; Lactose. DR CAZy; CBM13; Carbohydrate-Binding Module Family 13. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR UniLectin; P26514; -. DR BRENDA; 3.2.1.8; 6052. DR UniPathway; UPA00114; -. DR EvolutionaryTrace; P26514; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. 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 CDD; cd00161; RICIN; 1. DR Gene3D; 2.80.10.50; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR044846; GH10. DR InterPro; IPR031158; GH10_AS. DR InterPro; IPR001000; GH10_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR035992; Ricin_B-like_lectins. DR InterPro; IPR000772; Ricin_B_lectin. DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1. DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1. DR Pfam; PF00331; Glyco_hydro_10; 1. DR Pfam; PF00652; Ricin_B_lectin; 1. DR PRINTS; PR00134; GLHYDRLASE10. DR SMART; SM00633; Glyco_10; 1. DR SMART; SM00458; RICIN; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF50370; Ricin B-like lectins; 1. DR PROSITE; PS00591; GH10_1; 1. DR PROSITE; PS51760; GH10_2; 1. DR PROSITE; PS50231; RICIN_B_LECTIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing; KW Disulfide bond; Glycosidase; Hydrolase; Lectin; Polysaccharide degradation; KW Secreted; Signal; Xylan degradation. FT SIGNAL 1..41 FT /evidence="ECO:0000269|PubMed:1743521" FT CHAIN 42..477 FT /note="Endo-1,4-beta-xylanase A" FT /id="PRO_0000007979" FT DOMAIN 42..340 FT /note="GH10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096" FT DOMAIN 361..477 FT /note="Ricin B-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT ACT_SITE 169 FT /note="Proton donor" FT ACT_SITE 277 FT /note="Nucleophile" FT DISULFID 364..383 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174, FT ECO:0000269|PubMed:11914070" FT DISULFID 406..423 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174, FT ECO:0000269|PubMed:11914070" FT DISULFID 447..466 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174, FT ECO:0000269|PubMed:11914070" FT HELIX 46..51 FT /evidence="ECO:0007829|PDB:1V0L" FT TURN 52..54 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 69..78 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 80..86 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 90..93 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 103..114 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 118..125 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 132..135 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 139..156 FT /evidence="ECO:0007829|PDB:1V0L" FT TURN 157..160 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 162..168 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 183..186 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 191..202 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 206..214 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 221..236 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 242..245 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 251..253 FT /evidence="ECO:0007829|PDB:1OD8" FT HELIX 259..267 FT /evidence="ECO:0007829|PDB:1V0L" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 272..280 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 285..296 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 301..307 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 317..319 FT /evidence="ECO:0007829|PDB:1V0L" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:1V0L" FT HELIX 332..341 FT /evidence="ECO:0007829|PDB:1V0L" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:1KNL" FT STRAND 364..366 FT /evidence="ECO:0007829|PDB:1KNL" FT HELIX 368..370 FT /evidence="ECO:0007829|PDB:1KNL" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:1KNL" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:1KNL" FT STRAND 391..393 FT /evidence="ECO:0007829|PDB:1KNL" FT STRAND 399..401 FT /evidence="ECO:0007829|PDB:1KNL" FT TURN 402..404 FT /evidence="ECO:0007829|PDB:1KNL" FT STRAND 405..410 FT /evidence="ECO:0007829|PDB:1KNL" FT STRAND 417..422 FT /evidence="ECO:0007829|PDB:1KNL" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:1KNL" FT STRAND 431..433 FT /evidence="ECO:0007829|PDB:1KNL" FT STRAND 439..441 FT /evidence="ECO:0007829|PDB:1KNL" FT TURN 442..444 FT /evidence="ECO:0007829|PDB:1KNL" FT STRAND 447..450 FT /evidence="ECO:0007829|PDB:1KNL" FT HELIX 451..453 FT /evidence="ECO:0007829|PDB:1KNL" FT STRAND 460..464 FT /evidence="ECO:0007829|PDB:1KNL" FT HELIX 470..472 FT /evidence="ECO:0007829|PDB:1KNL" SQ SEQUENCE 477 AA; 51163 MW; E14A7FE37BDC68CC CRC64; MGSYALPRSG VRRSIRVLLL ALVVGVLGTA TALIAPPGAH AAESTLGAAA AQSGRYFGTA IASGRLSDST YTSIAGREFN MVTAENEMKI DATEPQRGQF NFSSADRVYN WAVQNGKQVR GHTLAWHSQQ PGWMQSLSGS ALRQAMIDHI NGVMAHYKGK IVQWDVVNEA FADGSSGARR DSNLQRSGND WIEVAFRTAR AADPSAKLCY NDYNVENWTW AKTQAMYNMV RDFKQRGVPI DCVGFQSHFN SGSPYNSNFR TTLQNFAALG VDVAITELDI QGAPASTYAN VTNDCLAVSR CLGITVWGVR DSDSWRSEQT PLLFNNDGSK KAAYTAVLDA LNGGDSSEPP ADGGQIKGVG SGRCLDVPDA STSDGTQLQL WDCHSGTNQQ WAATDAGELR VYGDKCLDAA GTSNGSKVQI YSCWGGDNQK WRLNSDGSVV GVQSGLCLDA VGNGTANGTL IQLYTCSNGS NQRWTRT //