XYNA_STRLI
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 25-MAY-2022, entry version 125.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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}.
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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 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; PTHR31490; 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; SSF50370; SSF50370; 1.
DR SUPFAM; SSF51445; SSF51445; 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
