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Database: UniProt
Entry: Q59674
LinkDB: Q59674
Original site: Q59674 
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   05-DEC-2018, entry version 87.
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
RT   modular architecture in xylanases from the aerobic soil bacteria
RT   Pseudomonas 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
CC       able to hydrolyze oat spelt xylan and the arabinoxylans from wheat
CC       and rye, releasing xylobiose as the major product. Also likely
CC       catalyzes, via its C-terminal domain, the removal of acetyl groups
CC       from acetylated xylan. Thus, has the capability of hydrolyzing
CC       acetylated xylan. Does not attack mannan, galactan, arabinan or
CC       any cellulosic substrates. {ECO:0000269|PubMed:12107129,
CC       ECO:0000269|PubMed:7492333}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; 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
CC       beta-glucan but not on medium containing mannan. Is repressed by
CC       glucose. Transcription of xyn11A occurs in early exponential
CC       phase, and thus earlier than transcription of xyn11B.
CC       {ECO:0000269|PubMed:12107129}.
CC   -!- DOMAIN: The N-terminal domain possesses xylanase activity, the
CC       central region likely has xylan deacetylase activity, and the
CC       small C-terminal 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}.
DR   EMBL; Z48927; CAA88763.1; -; Genomic_DNA.
DR   PIR; S59633; S59633.
DR   ProteinModelPortal; 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   mycoCLAP; XYN11E_CELJA; -.
DR   PRIDE; Q59674; -.
DR   eggNOG; ENOG4108ZJ4; Bacteria.
DR   eggNOG; COG0726; LUCA.
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;
KW   Multifunctional enzyme; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28    661       Bifunctional xylanase/xylan deacetylase.
FT                                /FTId=PRO_5000147608.
FT   DOMAIN       29    226       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   DOMAIN      398    574       NodB homology. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01014}.
FT   DOMAIN      616    645       CBM10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01099}.
FT   REGION      394    577       Polysaccharide deacetylase.
FT   COMPBIAS    228    401       Gly-rich.
FT   COMPBIAS    587    606       Ser-rich.
FT   ACT_SITE    116    116       Nucleophile; for endoxylanase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10062}.
FT   ACT_SITE    213    213       Proton donor; for endoxylanase activity.
FT                                {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
//
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