ID   XYNA_CALSA              Reviewed;         342 AA.
AC   P23556;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 93.
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;
GN   Name=xynA;
OS   Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=44001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2111111; DOI=10.1128/aem.56.4.1017-1024.1990;
RA   Luethi E., Love D.R., McAnulty J., Wallace C., Caughey P.A., Saul D.J.,
RA   Bergquist P.L.;
RT   "Cloning, sequence analysis, and expression of genes encoding xylan-
RT   degrading enzymes from the thermophile 'Caldocellum saccharolyticum'.";
RL   Appl. Environ. Microbiol. 56:1017-1024(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Te'O V.S. Jr., Gibbs M.D., Saul D.J., Bergquist P.L.;
RT   "A cluster of genes involved in xylan degradation cloned from the extreme
RT   thermophile Caldicellulosiruptor saccharolyticus.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=2275529; DOI=10.1128/aem.56.9.2677-2683.1990;
RA   Luethi E., Jasmat N.B., Bergquist P.L.;
RT   "Xylanase from the extremely thermophilic bacterium 'Caldocellum
RT   saccharolyticum': overexpression of the gene in Escherichia coli and
RT   characterization of the gene product.";
RL   Appl. Environ. Microbiol. 56:2677-2683(1990).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5-6.0.;
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       Cytoplasmic xylanase subfamily. {ECO:0000305}.
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DR   EMBL; M34459; AAA23059.1; -; Genomic_DNA.
DR   EMBL; AF005383; AAB87374.1; -; Genomic_DNA.
DR   PIR; A37202; A60154.
DR   AlphaFoldDB; P23556; -.
DR   SMR; P23556; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   PRIDE; P23556; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Xylan degradation.
FT   CHAIN           1..342
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000007984"
FT   DOMAIN          11..342
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        144
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   342 AA;  40455 MW;  C5380F2AB0CC0271 CRC64;
     MRCLIVCENL EMLNLSLAKT YKDYFKIGAA VTAKDLEGVH RDILLKHFNS LTPENAMKFE
     NIHPEEQRYN FEEVARIKEF AIKNDMKLRG HTFVWHNQTP GWVFLDKNGE EASKELVIER
     LREHIKTLCE RYKDVVYAWD VVNEAVEDKT EKLLRESNWR KIIGDDYIKI AFEIAREYAG
     DAKLFYNDYN NEMPYKLEKT YKVLKELLER GTPIDGIGIQ AHWNIWDKNL VSNLKKAIEV
     YASLGLEIHI TELDISVFEF EDKRTDLFEP TPEMLELQAK VYEDVFAVFR EYKDVITSVT
     LWGISDRHTW KDNFPVKGRK DWPLLFDVNG KPKEALYRIL RF