GenomeNet

Database: UniProt
Entry: P83513
LinkDB: P83513
Original site: P83513 
ID   XY11A_PSEXY             Reviewed;         602 AA.
AC   P83513;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   05-DEC-2018, entry version 79.
DE   RecName: Full=Bifunctional xylanase/deacetylase;
DE   Includes:
DE     RecName: Full=Endo-1,4-beta-xylanase 11A;
DE              EC=3.2.1.8;
DE     AltName: Full=Xylanase XynT;
DE     AltName: Full=Xylanase xyn11A;
DE   Includes:
DE     RecName: Full=Acetylated xylan deacetylase;
DE              EC=3.5.1.-;
DE   Flags: Precursor;
GN   Name=xyn11A; Synonyms=xynT;
OS   Pseudobutyrivibrio xylanivorans.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Pseudobutyrivibrio.
OX   NCBI_TaxID=185007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DOMAIN ORGANIZATION.
RC   STRAIN=Mz5T;
RX   PubMed=17007421; DOI=10.1007/BF02931809;
RA   Cepeljnik T., Rincon M.T., Flint H.J., Marinsek-Logar R.;
RT   "Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio
RT   xylanivorcans Mz5T.";
RL   Folia Microbiol. (Praha) 51:263-267(2006).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-193, PROTEIN SEQUENCE OF
RP   15-39, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC   STRAIN=Mz5T;
RA   Cepeljnik T., Krizaj I., Marinsek-Logar R.;
RT   "Isolation and characterization of the Pseudobutyrivibrio xylanivorans
RT   Mz5T xylanase XynT -- the first family 11 endoxylanase from rumen
RT   Butyrivibrio-related bacteria.";
RL   Enzyme Microb. Technol. 34:219-227(2004).
CC   -!- FUNCTION: Endo-acting xylanase which specifically cleaves internal
CC       linkages on the xylan backbone, releasing xylooligosaccharides. Is
CC       also probably able, via its C-terminal domain, to remove acetyl
CC       groups from acetylated xylan, and thus it is probably capable of
CC       hydrolyzing acetylated xylan. {ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8; Evidence={ECO:0000269|Ref.2};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.6. Active from pH 4.0 to 8.0.;
CC       Temperature dependence:
CC         Optimum temperature is 38 degrees Celsius.;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2, ECO:0000305}.
CC   -!- DOMAIN: Consists of three domains: two complementary catalytic
CC       domains and one substrate-binding module.
CC       {ECO:0000269|PubMed:17007421}.
CC   -!- PTM: In the later growth phases, seems to undergo a proteolytic
CC       cleavage into a 30 kDa protein possessing xylanolytic activity.
CC   -!- BIOTECHNOLOGY: Could be used as a feed additive for animals in
CC       order to diminish health problems due to undigested plant fiber
CC       and enhance proliferation of beneficial microflora.
CC       {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; AJ543424; CAD65888.2; -; Genomic_DNA.
DR   ProteinModelPortal; P83513; -.
DR   SMR; P83513; -.
DR   CAZy; CBM36; Carbohydrate-Binding Module Family 36.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11T_PSEXY; -.
DR   PRIDE; P83513; -.
DR   BioCyc; MetaCyc:MONOMER-17647; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_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; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR002509; NODB_dom.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Multifunctional enzyme; Polysaccharide degradation;
KW   Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     14       {ECO:0000269|Ref.2}.
FT   CHAIN        15    602       Bifunctional xylanase/deacetylase.
FT                                /FTId=PRO_0000184070.
FT   DOMAIN       17    211       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   DOMAIN      249    366       CBM6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00523}.
FT   DOMAIN      402    578       NodB homology. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01014}.
FT   ACT_SITE    108    108       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    198    198       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
SQ   SEQUENCE   602 AA;  65923 MW;  F3D7AE32EF7A3CF0 CRC64;
     MSATLLVPSM TVKAADTIYN NKTGNQDGYD YELWKDTGNT SMTLNAGGTF DCSWSNINNA
     LFRKGKKFDS TQTYQQIGNI TFDYGCDYRP NGNSYLCVYG WTVDPLVEYY IVDSWGTWRP
     PGGTPKGQIQ VDGGTYDVYE TTRYNAPSIQ GDTTFKQYFS VRTSKRTSGT ISVSEHFKAW
     ERMGMRCGNF MKPALNIEGY QSSGSASVYK NNMTIGGSSS SSGNQGGNQG GNTGNENAGN
     NLVTVADADK IQCETMTKSG QYTGNISSPF NGVALYANND AVKYTQYFAS GTHDFTLRGC
     SNNNKMARVD LKIGGQNKGT FYYGDSYPAE YTIKNVSHGT GNQTIELVVT ADDGQWDAYL
     DYFNNSVEPG CSLVPGAVVV LVALGSSSNT GNNSGTNTQN QKLIALTFDD GPSSTTSQVL
     DMLEKYNVKA TFFLIGQNVN SNTASIVQRQ VKMGCELACH SYTHEDMTKM NASQIRNQID
     WTASAIKNTA GVDVKFFRPP YISVNNTMYQ NIDLPFIQGS MHNDWESSTS ASQRVNSVLS
     SAKDGDIILL HDFQGNSQTV SALPQIIEGL KNQGYTFVTV SELFEMKGVN PNVEYKIWSN
     VK
//
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