XY11A_PSEXY
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 03-AUG-2022, entry version 89.
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; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=185007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DOMAIN ORGANIZATION.
RC STRAIN=ATCC BAA-455 / DSM 14809 / Mz 5;
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 15-39,
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND BIOTECHNOLOGY.
RC STRAIN=ATCC BAA-455 / DSM 14809 / Mz 5;
RA Cepeljnik T., Krizaj I., Marinsek-Logar R.;
RT "Isolation and characterization of the Pseudobutyrivibrio xylanivorans Mz5T
RT xylanase XynT -- the first family 11 endoxylanase from rumen Butyrivibrio-
RT 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 also
CC probably able, via its C-terminal domain, to remove acetyl groups from
CC acetylated xylan, and thus it is probably capable of hydrolyzing
CC acetylated xylan. {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC 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 domains
CC and one substrate-binding module. {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 order to
CC diminish health problems due to undigested plant fiber and enhance
CC proliferation of beneficial microflora. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; AJ543424; CAD65888.2; -; Genomic_DNA.
DR AlphaFoldDB; P83513; -.
DR SMR; P83513; -.
DR CAZy; CBM36; Carbohydrate-Binding Module Family 36.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11T_PSEXY; -.
DR BioCyc; MetaCyc:MON-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 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; Hydrolase;
KW Multifunctional enzyme; Polysaccharide degradation; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..14
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 15..602
FT /note="Bifunctional xylanase/deacetylase"
FT /id="PRO_0000184070"
FT DOMAIN 17..211
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT DOMAIN 249..366
FT /note="CBM6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT DOMAIN 402..578
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT REGION 216..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-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
