XY10C_CELJA
ID XY10C_CELJA Reviewed; 606 AA.
AC Q59675;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Endo-beta-1,4-xylanase Xyn10C;
DE Short=Xylanase 10C;
DE EC=3.2.1.8;
DE AltName: Full=XYLF;
DE Flags: Precursor;
GN Name=xyn10C; Synonyms=xynF;
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, CATALYTIC ACTIVITY, SUBSTRATE
RP 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 SEQUENCE REVISION.
RA Gilbert H.J.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP 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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 91-243 IN COMPLEX WITH
RP XYLOPENTAOSE, DISULFIDE BOND, AND DOMAIN.
RX PubMed=11598143; DOI=10.1074/jbc.m109558200;
RA Szabo L., Jamal S., Xie H., Charnock S.J., Bolam D.N., Gilbert H.J.,
RA Davies G.J.;
RT "Structure of a family 15 carbohydrate-binding module in complex with
RT xylopentaose. Evidence that xylan binds in an approximate 3-fold helical
RT conformation.";
RL J. Biol. Chem. 276:49061-49065(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 86-606 OF WILD-TYPE AND MUTANT
RP ALA-385 IN COMPLEX WITH XYLOTETRAOSE, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, ACTIVE SITE, DOMAIN, AND MUTAGENESIS OF TYR-340.
RX PubMed=14670951; DOI=10.1074/jbc.m311947200;
RA Pell G., Szabo L., Charnock S.J., Xie H., Gloster T.M., Davies G.J.,
RA Gilbert H.J.;
RT "Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C:
RT how variation in substrate-binding cleft influences the catalytic profile
RT of family GH-10 xylanases.";
RL J. Biol. Chem. 279:11777-11788(2004).
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, the arabinoxylans from wheat and rye, and
CC glucuronoxylan. Also displays very low activity against
CC xylooligosaccharides. During the xylan degradation process, Xyn10C may
CC act on the soluble xylans and long xylooligosaccharides products
CC released by the secreted xylanases Xyn11A, Xyn11B and Xyn10A.
CC {ECO:0000269|PubMed:14670951, 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:14670951,
CC ECO:0000269|PubMed:7492333};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:12107129}; Lipid-anchor
CC {ECO:0000305|PubMed:12107129}. Note=Is predominantly associated with
CC the cell membrane.
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 {ECO:0000269|PubMed:12107129}.
CC -!- DOMAIN: The N-terminal CBM15 domain binds xylan, including decorated
CC xylans and xylooligosaccharides, but the physiological role of this
CC domain is unclear. It may act as a product capture system: large
CC xylooligosaccharides generated by Xyn10C would bind to CBM15 and this
CC would restrict the diffusion of these polymers into the environment and
CC therefore increase the selective utilization of these molecules by
CC C.japonicus. Xylanase activity resides in the C-terminal domain.
CC {ECO:0000269|PubMed:11598143, ECO:0000269|PubMed:14670951,
CC ECO:0000269|PubMed:7492333}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; Z48928; CAA88764.2; -; Genomic_DNA.
DR PIR; S59634; S59634.
DR RefSeq; WP_012488644.1; NZ_CP043306.1.
DR PDB; 1GNY; X-ray; 1.63 A; A=91-243.
DR PDB; 1US2; X-ray; 1.85 A; A=86-606.
DR PDB; 1US3; X-ray; 1.85 A; A=86-606.
DR PDBsum; 1GNY; -.
DR PDBsum; 1US2; -.
DR PDBsum; 1US3; -.
DR AlphaFoldDB; Q59675; -.
DR SMR; Q59675; -.
DR DrugBank; DB03389; alpha-D-Xylopyranose.
DR CAZy; CBM15; Carbohydrate-Binding Module Family 15.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR BRENDA; 3.2.1.8; 5103.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; Q59675; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR005088; CBM_fam15.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; PF03426; CBM_15; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51759; CBM15; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell outer membrane; Disulfide bond;
KW Glycosidase; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW Polysaccharide degradation; Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..606
FT /note="Endo-beta-1,4-xylanase Xyn10C"
FT /id="PRO_5000147609"
FT DOMAIN 91..242
FT /note="CBM15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01095"
FT DOMAIN 245..596
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT REGION 23..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 385
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 497
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:14670951"
FT BINDING 106
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 171
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 217
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 296..299
FT /ligand="substrate"
FT BINDING 332
FT /ligand="substrate"
FT BINDING 384
FT /ligand="substrate"
FT BINDING 552
FT /ligand="substrate"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT DISULFID 183..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01095,
FT ECO:0000269|PubMed:11598143"
FT MUTAGEN 340
FT /note="Y->A: Significantly reduces the catalytic activity
FT against xylotetraose and xylan. Also modifies the cleavage
FT pattern of xylotetraose."
FT /evidence="ECO:0000269|PubMed:14670951"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1GNY"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1GNY"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:1GNY"
FT STRAND 228..242
FT /evidence="ECO:0007829|PDB:1GNY"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:1US2"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:1US2"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 353..374
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 401..405
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 412..423
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 427..435
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 441..455
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 476..487
FT /evidence="ECO:0007829|PDB:1US2"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 492..503
FT /evidence="ECO:0007829|PDB:1US2"
FT TURN 508..513
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 520..540
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 546..552
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 560..564
FT /evidence="ECO:0007829|PDB:1US2"
FT TURN 565..571
FT /evidence="ECO:0007829|PDB:1US2"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:1US2"
FT HELIX 588..598
FT /evidence="ECO:0007829|PDB:1US2"
SQ SEQUENCE 606 AA; 64884 MW; 56E149954CE6BFEE CRC64;
MKKIQQLLML SLISSTLIAC GGGGGGGSTP TTSSSPQSSS PASTPSSASS SSIISSSSLS
SSLSSSSLSS SSLSSSSASS VSSSSVAASE GNVVIEVDMA NGWRGNASGS TSHSGITYSA
DGVTFAALGD GVGAVFDIAR PTTLEDAVIA MVVNVSAEFK ASEANLQIFA QLKEDWSKGE
WDCLAASSEL TADTDLTLTC TIDEDDDKFN QTARDVQVGI QAKGTPAGTI TIKSVTITLA
QEAYSANVDH LRDLAPSDFP IGVAVSNTDS ATYNLLTNSR EQAVVKKHFN HLTAGNIMKM
SYMQPTEGNF NFTNADAFVD WATENNMTVH GHALVWHSDY QVPNFMKNWA GSAEDFLAAL
DTHITTIVDH YEAKGNLVSW DVVNEAIDDN SPANFRTTDS AFYVKSGNSS VYIERAFQTA
RAADPAVILY YNDYNIEQNN AKTTKMVDMV KDFQARSIPI DGVGFQMHVC MNYPSIANIS
AAMKKVVDLG LLVKITELDV AVNQPHCDAY PANKINPLTE AAQLAQKKRY CDVVKAYLDT
VPVNQRGGIS VWGTTDANTW LDGLYREQFE DEKISWPLLF DNNYNDKPAL RGFADALIGT
QCTNTH
