ID   XY11A_CELJA             Reviewed;         661 AA.
AC   Q59674;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Bifunctional xylanase/xylan deacetylase;
DE   AltName: Full=XYLE;
DE   Includes:
DE     RecName: Full=Endo-1,4-beta-xylanase Xyn11A;
DE              Short=Xylanase 11A;
DE              EC=3.2.1.8;
DE   Includes:
DE     RecName: Full=Acetylxylan deacetylase;
DE              EC=3.1.1.72;
DE   Flags: Precursor;
GN   Name=xyn11A; Synonyms=xynE;
OS   Cellvibrio japonicus (Pseudomonas fluorescens subsp. cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=155077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A XYLANASE, CATALYTIC
RP   ACTIVITY, SUBSTRATE SPECIFICITY, AND DOMAIN.
RC   STRAIN=NCIMB 10462;
RX   PubMed=7492333; DOI=10.1042/bj3120039;
RA   Millward-Sadler S.J., Davidson K., Hazlewood G.P., Black G.W.,
RA   Gilbert H.J., Clarke J.H.;
RT   "Novel cellulose-binding domains, NodB homologues and conserved modular
RT   architecture in xylanases from the aerobic soil bacteria Pseudomonas
RT   fluorescens subsp. cellulosa and Cellvibrio mixtus.";
RL   Biochem. J. 312:39-48(1995).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=12107129; DOI=10.1128/jb.184.15.4124-4133.2002;
RA   Emami K., Nagy T., Fontes C.M., Ferreira L.M., Gilbert H.J.;
RT   "Evidence for temporal regulation of the two Pseudomonas cellulosa
RT   xylanases belonging to glycoside hydrolase family 11.";
RL   J. Bacteriol. 184:4124-4133(2002).
CC   -!- FUNCTION: Endo-acting xylanase which specifically cleaves internal
CC       linkages on the xylan backbone, releasing xylooligosaccharides. Is able
CC       to hydrolyze oat spelt xylan and the arabinoxylans from wheat and rye,
CC       releasing xylobiose as the major product. Also likely catalyzes, via
CC       its C-terminal domain, the removal of acetyl groups from acetylated
CC       xylan. Thus, has the capability of hydrolyzing acetylated xylan. Does
CC       not attack mannan, galactan, arabinan or any cellulosic substrates.
CC       {ECO:0000269|PubMed:12107129, ECO:0000269|PubMed:7492333}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000269|PubMed:7492333};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC         EC=3.1.1.72; Evidence={ECO:0000269|PubMed:7492333};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12107129}.
CC   -!- INDUCTION: Induced when the bacterium is cultured on xylan or beta-
CC       glucan but not on medium containing mannan. Is repressed by glucose.
CC       Transcription of xyn11A occurs in early exponential phase, and thus
CC       earlier than transcription of xyn11B. {ECO:0000269|PubMed:12107129}.
CC   -!- DOMAIN: The N-terminal domain possesses xylanase activity, the central
CC       region likely has xylan deacetylase activity, and the small C-terminal
CC       domain is involved in carbohydrate-binding.
CC       {ECO:0000269|PubMed:7492333}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glycosyl
CC       hydrolase 11 (cellulase G) family. {ECO:0000305}.
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DR   EMBL; Z48927; CAA88763.1; -; Genomic_DNA.
DR   PIR; S59633; S59633.
DR   RefSeq; WP_012489333.1; NZ_CP043306.1.
DR   AlphaFoldDB; Q59674; -.
DR   SMR; Q59674; -.
DR   CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR   CAZy; CBM60; Carbohydrate-Binding Module Family 60.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11E_CELJA; -.
DR   OMA; YSETMHC; -.
DR   SABIO-RK; Q59674; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose 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; 2.30.32.30; -; 1.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR036601; CBM10_sf.
DR   InterPro; IPR031768; CBM60_xylan-bd.
DR   InterPro; IPR009031; CBM_fam10.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
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; PF16841; CBM60; 1.
DR   Pfam; PF02013; CBM_10; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM01064; CBM_10; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF57615; SSF57615; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   PROSITE; PS51763; CBM10; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS51761; GH11_3; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Multifunctional enzyme;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..661
FT                   /note="Bifunctional xylanase/xylan deacetylase"
FT                   /id="PRO_5000147608"
FT   DOMAIN          29..226
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   DOMAIN          398..574
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT   DOMAIN          616..645
FT                   /note="CBM10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   REGION          220..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..577
FT                   /note="Polysaccharide deacetylase"
FT   REGION          578..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        116
FT                   /note="Nucleophile; for endoxylanase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        213
FT                   /note="Proton donor; for endoxylanase activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   661 AA;  69193 MW;  3D8C897D4C732FEB CRC64;
     MKLPTLGKCV VRTLMGAVAL GAISVNAQTL SSNSTGTNNG FYYTFWKDSG DASMTLLSGG
     RYQSSWGNST NNWVGGKGWN PGNNSRVISY SGSYGVDSSQ NSYLALYGWT RSPLIEYYVI
     ESYGSYNPAS CSGGTDYGSF QSDGATYNVR RCQRVNQPSI DGTQTFYQYF SVRNPKKGFG
     NISGTITFAN HVNFWASKGL NLGNHNYQVL ATEGYQSRGS SDITVSEGTS GGGTSSVGGA
     SSSVNSSTGG GSSGGITVRA RGANGSEHIN LRVGGAVVAN WTLGTSFQNY LYSGNASGDI
     QVQFDNDASG RDVVVDYIIV NGETRQAEDM EHNSAVYANG RCGGGSYSEN MHCNGEIGFG
     YTYDCFSGNC SGGNGGSNSS AGNSSSGNTG GGGSNCSGYV GITFDDGPNS NTATLVNLLR
     QNNLTPVTWF NQGNNVASNA HLMSQQLSVG EVHNHSYTHP HMTSWTYQQV YDELNRTNQA
     IQNAGAPKPT LFRPPYGELN STIQQAAQAL GLRVVTWDVD SQDWNGASAA AIANAANQLQ
     NGQVILMHDG SYTNTNSAIA QIATNLRAKG LCPGRIDPNT GRAVAPSSSG GSSSVALSSS
     SRSSSSAGGN TGGNCQCNWW GTFYPLCQTQ TSGWGWENSR SCISTSTCNS QGTGGGGVVC
     N