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 28-JUN-2023, entry version 102.
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; Bacillota; 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 AlphaFoldDB; P17137; -.
DR SMR; P17137; -.
DR STRING; 169679.CSACC_19880; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11B_CLOSA; -.
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 PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//
