XYNA_CELJU
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 25-MAY-2022, entry version 160.
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 Pseudomonas
RT fluorescens subspecies cellulosa: internal signal sequence and unusual
RT 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 the
RT 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 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 Pseudomonas
RT fluorescens and identification of the xylopentaose-binding 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 Pseudomonas
RT xylanase A.";
RL Biochemistry 39:978-984(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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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 AlphaFoldDB; 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; COG3693; Bacteria.
DR HOGENOM; CLU_029617_0_0_6; -.
DR OMA; GADDWPL; -.
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; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
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; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Signal; Xylan degradation.
FT SIGNAL 1..26
FT CHAIN 27..611
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000007977"
FT DOMAIN 27..128
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT DOMAIN 183..212
FT /note="CBM10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT DOMAIN 281..607
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 391
FT /note="Proton donor"
FT ACT_SITE 510
FT /note="Nucleophile"
FT DISULFID 31..125
FT /evidence="ECO:0000250"
FT DISULFID 184..215
FT /evidence="ECO:0000269|PubMed:10653641"
FT DISULFID 194..209
FT /evidence="ECO:0000269|PubMed:10653641"
FT CONFLICT 432..433
FT /note="RA -> PR (in Ref. 1; CAA33469)"
FT /evidence="ECO:0000305"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1E8R"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1E8R"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1E8R"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1E8R"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:1E8R"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:1W32"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1CLX"
FT HELIX 364..378
FT /evidence="ECO:0007829|PDB:1W32"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 422..434
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 452..466
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 487..498
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 505..515
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:1W3H"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 530..533
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 538..557
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:1W2V"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:1W32"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:1W32"
FT HELIX 599..609
FT /evidence="ECO:0007829|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
