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Database: UniProt
Entry: P14768
LinkDB: P14768
Original site: P14768 
ID   XYNA_CELJU              Reviewed;         611 AA.
AC   P14768; B3PKK3;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   28-MAR-2018, entry version 147.
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;
DE            Short=XYLA;
DE   Flags: Precursor;
GN   Name=xynA; Synonyms=xyn10A; OrderedLocusNames=CJA_2471;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2507868; DOI=10.1111/j.1365-2958.1989.tb00271.x;
RA   Hall J., Hazlewood G.P., Huskisson N.S., Durrant A.J., Gilbert H.J.;
RT   "Conserved serine-rich sequences in xylanase and cellulase from
RT   Pseudomonas fluorescens subspecies cellulosa: internal signal sequence
RT   and unusual protein processing.";
RL   Mol. Microbiol. 3:1211-1219(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/JB.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of
RT   the soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 265-611, AND SEQUENCE
RP   REVISION.
RX   PubMed=7881909; DOI=10.1016/S0969-2126(94)00112-X;
RA   Harris G.W., Jenkins J.A., Connerton I., Cummings N., Lo Leggio L.,
RA   Scott M., Hazlewood G.P., Laurie J.I., Gilbert H.J., Pickersgill R.W.;
RT   "Structure of the catalytic core of the family F xylanase from
RT   Pseudomonas fluorescens and identification of the xylopentaose-binding
RT   sites.";
RL   Structure 2:1107-1116(1994).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 265-611.
RX   PubMed=15299710; DOI=10.1107/S0907444995013540;
RA   Harris G.W., Jenkins J.A., Connerton I., Pickersgill R.W.;
RT   "Refined crystal structure of the catalytic domain of xylanase A from
RT   Pseudomonas fluorescens at 1.8-A resolution.";
RL   Acta Crystallogr. D 52:393-401(1996).
RN   [5]
RP   STRUCTURE BY NMR OF 180-228, AND DISULFIDE BONDS.
RX   PubMed=10653641; DOI=10.1021/bi992163+;
RA   Raghothama S., Simpson P.J., Szabo L., Nagy T., Gilbert H.J.,
RA   Williamson M.P.;
RT   "Solution structure of the CBM10 cellulose binding module from
RT   Pseudomonas xylanase A.";
RL   Biochemistry 39:978-984(2000).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans.
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
DR   EMBL; X15429; CAA33469.1; -; Genomic_DNA.
DR   EMBL; CP000934; ACE85439.1; -; Genomic_DNA.
DR   PIR; S06047; S06047.
DR   PDB; 1CLX; X-ray; 1.80 A; A/B/C/D=265-611.
DR   PDB; 1E5N; X-ray; 3.20 A; A/B=264-611.
DR   PDB; 1E8R; NMR; -; A=180-228.
DR   PDB; 1QLD; NMR; -; A=180-228.
DR   PDB; 1W2P; X-ray; 1.45 A; A/B=265-611.
DR   PDB; 1W2V; X-ray; 1.55 A; A/B=265-611.
DR   PDB; 1W32; X-ray; 1.20 A; A/B=265-611.
DR   PDB; 1W3H; X-ray; 1.50 A; A/B=265-611.
DR   PDB; 1XYS; X-ray; 2.50 A; A/B=265-611.
DR   PDBsum; 1CLX; -.
DR   PDBsum; 1E5N; -.
DR   PDBsum; 1E8R; -.
DR   PDBsum; 1QLD; -.
DR   PDBsum; 1W2P; -.
DR   PDBsum; 1W2V; -.
DR   PDBsum; 1W32; -.
DR   PDBsum; 1W3H; -.
DR   PDBsum; 1XYS; -.
DR   ProteinModelPortal; P14768; -.
DR   SMR; P14768; -.
DR   STRING; 498211.CJA_2471; -.
DR   CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EnsemblBacteria; ACE85439; ACE85439; CJA_2471.
DR   KEGG; cja:CJA_2471; -.
DR   eggNOG; ENOG4106J46; Bacteria.
DR   eggNOG; COG3693; LUCA.
DR   HOGENOM; HOG000066328; -.
DR   KO; K01181; -.
DR   OMA; GADDWPL; -.
DR   OrthoDB; POG091H0Y2G; -.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P14768; -.
DR   Proteomes; UP000001036; Chromosome.
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:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.30.32.30; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR036601; CBM10_sf.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR009031; CBM_fam10.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02013; CBM_10; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM01064; CBM_10; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57615; SSF57615; 1.
DR   PROSITE; PS51763; CBM10; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     26
FT   CHAIN        27    611       Endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000007977.
FT   DOMAIN       27    128       CBM2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01135}.
FT   DOMAIN      183    212       CBM10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01099}.
FT   DOMAIN      281    607       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   COMPBIAS    131    179       Ser-rich (linker).
FT   COMPBIAS    227    259       Ser-rich.
FT   ACT_SITE    391    391       Proton donor.
FT   ACT_SITE    510    510       Nucleophile.
FT   DISULFID     31    125       {ECO:0000250}.
FT   DISULFID    184    215       {ECO:0000269|PubMed:10653641}.
FT   DISULFID    194    209       {ECO:0000269|PubMed:10653641}.
FT   CONFLICT    432    433       RA -> PR (in Ref. 1; CAA33469).
FT                                {ECO:0000305}.
FT   STRAND      183    186       {ECO:0000244|PDB:1E8R}.
FT   STRAND      189    193       {ECO:0000244|PDB:1E8R}.
FT   STRAND      199    204       {ECO:0000244|PDB:1E8R}.
FT   STRAND      207    210       {ECO:0000244|PDB:1E8R}.
FT   HELIX       212    215       {ECO:0000244|PDB:1E8R}.
FT   HELIX       266    269       {ECO:0000244|PDB:1W32}.
FT   STRAND      274    279       {ECO:0000244|PDB:1W32}.
FT   STRAND      281    283       {ECO:0000244|PDB:1W32}.
FT   TURN        287    289       {ECO:0000244|PDB:1W32}.
FT   HELIX       291    300       {ECO:0000244|PDB:1W32}.
FT   STRAND      302    308       {ECO:0000244|PDB:1W32}.
FT   HELIX       312    315       {ECO:0000244|PDB:1W32}.
FT   HELIX       324    335       {ECO:0000244|PDB:1W32}.
FT   STRAND      339    346       {ECO:0000244|PDB:1W32}.
FT   HELIX       350    352       {ECO:0000244|PDB:1W32}.
FT   STRAND      358    360       {ECO:0000244|PDB:1CLX}.
FT   HELIX       364    378       {ECO:0000244|PDB:1W32}.
FT   TURN        379    382       {ECO:0000244|PDB:1W32}.
FT   STRAND      384    390       {ECO:0000244|PDB:1W32}.
FT   HELIX       396    398       {ECO:0000244|PDB:1W32}.
FT   HELIX       413    418       {ECO:0000244|PDB:1W32}.
FT   HELIX       422    434       {ECO:0000244|PDB:1W32}.
FT   STRAND      438    446       {ECO:0000244|PDB:1W32}.
FT   HELIX       452    466       {ECO:0000244|PDB:1W32}.
FT   STRAND      473    476       {ECO:0000244|PDB:1W32}.
FT   STRAND      479    485       {ECO:0000244|PDB:1W32}.
FT   HELIX       487    498       {ECO:0000244|PDB:1W32}.
FT   STRAND      505    515       {ECO:0000244|PDB:1W32}.
FT   HELIX       518    520       {ECO:0000244|PDB:1W3H}.
FT   STRAND      523    525       {ECO:0000244|PDB:1W32}.
FT   HELIX       530    533       {ECO:0000244|PDB:1W32}.
FT   HELIX       538    557       {ECO:0000244|PDB:1W32}.
FT   HELIX       560    562       {ECO:0000244|PDB:1W2V}.
FT   STRAND      563    569       {ECO:0000244|PDB:1W32}.
FT   HELIX       573    575       {ECO:0000244|PDB:1W32}.
FT   STRAND      579    581       {ECO:0000244|PDB:1W32}.
FT   STRAND      589    591       {ECO:0000244|PDB:1W32}.
FT   HELIX       599    609       {ECO:0000244|PDB:1W32}.
SQ   SEQUENCE   611 AA;  64804 MW;  2CFAA3D453E6B68E CRC64;
     MRTAMAKSLG AAAFLGAALF AHTLAAQTAT CSYNITNEWN TGYTGDITIT NRGSSAINGW
     SVNWQYATNR LSSSWNANVS GSNPYSASNL SWNGNIQPGQ SVSFGFQVNK NGGSAERPSV
     GGSICSGSVA SSSAPASSVP SSIASSSPSS VASSVISSMA SSSPVSSSSV ASSTPGSSSG
     NQQCNWYGTL YPLCVTTTNG WGWEDQRSCI ARSTCAAQPA PFGIVGSGSS TPVSSSSSSL
     SSSSVVSSIR SSSSSSSSSV ATGNGLASLA DFPIGVAVAA SGGNADIFTS SARQNIVRAE
     FNQITAENIM KMSYMYSGSN FSFTNSDRLV SWAAQNGQTV HGHALVWHPS YQLPNWASDS
     NANFRQDFAR HIDTVAAHFA GQVKSWDVVN EALFDSADDP DGRGSANGYR QSVFYRQFGG
     PEYIDEAFRR ARAADPTAEL YYNDFNTEEN GAKTTALVNL VQRLLNNGVP IDGVGFQMHV
     MNDYPSIANI RQAMQKIVAL SPTLKIKITE LDVRLNNPYD GNSSNDYTNR NDCAVSCAGL
     DRQKARYKEI VQAYLEVVPP GRRGGITVWG IADPDSWLYT HQNLPDWPLL FNDNLQPKPA
     YQGVVEALSG R
//
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