ID XYNA_CALSR Reviewed; 684 AA.
AC P40944;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=xynA;
OS Caldicellulosiruptor sp. (strain Rt8B.4).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=28238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8920183; DOI=10.1007/s002530050653;
RA Dwivedi P.P., Gibbs M.D., Saul D.J., Bergquist P.L.;
RT "Cloning, sequencing and overexpression in Escherichia coli of a xylanase
RT gene, xynA from the thermophilic bacterium Rt8B.4 genus
RT Caldicellulosiruptor.";
RL Appl. Microbiol. Biotechnol. 45:86-93(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 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; L18965; AAB42044.1; -; Genomic_DNA.
DR PIR; S41788; S41788.
DR AlphaFoldDB; P40944; -.
DR SMR; P40944; -.
DR CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
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; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF02018; CBM_4_9; 2.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Repeat; Signal; Xylan degradation.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..684
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000007981"
FT DOMAIN 40..190
FT /note="CBM-cenC 1"
FT DOMAIN 193..342
FT /note="CBM-cenC 2"
FT DOMAIN 350..678
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 490
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 598
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 684 AA; 78354 MW; 0AE575F4FB4BA5E6 CRC64;
MMRSLKSRKL VFILAMLFLI NAIVSLKFIT YSSANQLASK SKYIEYNFEN KSVSPLAKYP
SNVVLKVTNS TCAEGTFSVL VAGRKNANDG VIVDITKFLD FSREYEVSFY VLQTTKKLQR
ISVTLEILDS NDKNQVIAAE KVLLPNIWTK VSAKVQASNY KKAKRINLIV NMPTSKSDSF
YIDLFTIKDL ENAYVLKQEN FENKNTGGFL PEDKNCKITL AKDRAYSSAY SLKVQPSQKT
KNGKILFPIK GLLQKGGTYD FSLLVYQDSS KPVNFSAGIK LNDGKSTKEI VLAKQNVAPK
KWTQLFATLD LDTRFSAKDV SFFVKPAAAI SYYLDLYSIS DENWGQPVPD YNLPSLCEKY
KNYFKIGVAV PYRALTNPVD VEVIKRHFNS ITPENEMKPE SLQPYEGGFS FSIADEYVDF
CKKDNISLRG HTLVWHQQTP SWFFTNPETG EKLTNSEKDK EILLDRLKKH IQTVVGRYKG
KVYAWDVVNE AIDENQPDGY RRSDWYNILG PEYIEKAFIW AHEADPKAKL FYNDYSTEDP
YKREFIYKLI KNLKAKGVPV HGVGLQCHIS LDWPDVSEIE ETVKLFSRIP GLEIHFTEID
ISIAKNMTDD DAYNRYLLVQ QAQKLKAIFD VLKKYRNVVT SVTFWGLKDD YSWLRGDMPL
LSDKDYQPKF AFWSLIDPSV VPKE
//
