ID   XYNA_CLOSA              Reviewed;         261 AA.
AC   P17137;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=xynB;
OS   Clostridium saccharobutylicum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=169679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-117 / DSM 13864 / NCP 262;
RX   PubMed=2336398; DOI=10.1093/nar/18.8.2179;
RA   Zappe H., Jones W.A., Woods D.R.;
RT   "Nucleotide sequence of a Clostridium acetobutylicum P262 xylanase gene
RT   (xynB).";
RL   Nucleic Acids Res. 18:2179-2179(1990).
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}.
CC   -!- CAUTION: Was originally thought to originate from C.acetobutylicum.
CC       {ECO:0000305|PubMed:2336398}.
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DR   EMBL; M31726; AAA23287.1; -; Genomic_DNA.
DR   RefSeq; WP_022745983.1; NZ_LZZA01000111.1.
DR   AlphaFoldDB; P17137; -.
DR   SMR; P17137; -.
DR   STRING; 169679.CSACC_19880; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11B_CLOSA; -.
DR   GeneID; 55474453; -.
DR   UniPathway; UPA00114; -.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal; Xylan degradation.
FT   SIGNAL          1..28
FT   CHAIN           29..261
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /id="PRO_0000008001"
FT   DOMAIN          61..255
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        152
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        242
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
SQ   SEQUENCE   261 AA;  29033 MW;  339C3616F6FD14AE CRC64;
     MLRRKVIFTV LATLVMTSLT IVDNTAFAAT NLNTTESTFS KEVLSTQKTY SAFNTQAAPK
     TITSNEIGVN GGYDYELWKD YGNTSMTLKN GGAFSCQWSN IGNALFRKGK KFNDTQTYKQ
     LGNISVNYDC NYQPYGNSYL CVYGWTSSPL VEYYIVDSWG SWRPPGGTSK GTITVDGGIY
     DIYETTRINQ PSIQGNTTFK QYWSVRRTKR TSGTISVSKH FAAWESKGMP LGKMHETAFN
     IEGYQSSGKA DVNSMSINIG K