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Database: UniProt
Entry: Q00177
LinkDB: Q00177
Original site: Q00177 
ID   XYNC_EMENI              Reviewed;         327 AA.
AC   Q00177; C8VPM8; Q1HFU9; Q5BCB2;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   20-JUN-2018, entry version 119.
DE   RecName: Full=Endo-1,4-beta-xylanase C;
DE            Short=Xylanase C;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase C;
DE   AltName: Full=34 kDa xylanase;
DE   AltName: Full=Xylanase X34;
DE   Flags: Precursor;
GN   Name=xlnC; ORFNames=AN1818;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX   PubMed=8917072; DOI=10.1016/0378-1119(96)00116-3;
RA   Maccabe A.P., Fernandez-Espinar M.-T., de Graaff L.H., Visser J.,
RA   Ramon D.;
RT   "Identification, isolation and sequence of the Aspergillus nidulans
RT   xlnC gene encoding the 34-kDa xylanase.";
RL   Gene 175:29-33(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA   Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT   "Development and application of a suite of polysaccharide-degrading
RT   enzymes for analyzing plant cell walls.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 25-327 IN COMPLEX WITH WHEAT
RP   XIP-1, AND DISULFIDE BOND.
RX   PubMed=15181003; DOI=10.1074/jbc.M404225200;
RA   Payan F., Leone P., Porciero S., Furniss C., Tahir T., Williamson G.,
RA   Durand A., Manzanares P., Gilbert H.J., Juge N., Roussel A.;
RT   "The dual nature of the wheat xylanase protein inhibitor XIP-I:
RT   structural basis for the inhibition of family 10 and family 11
RT   xylanases.";
RL   J. Biol. Chem. 279:36029-36037(2004).
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of
CC       xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide
CC       in the biosphere, after cellulose. {ECO:0000269|PubMed:16844780,
CC       ECO:0000269|PubMed:8917072}.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.9. {ECO:0000269|PubMed:16844780};
CC       Temperature dependence:
CC         Optimum temperature is 52 degrees Celsius.
CC         {ECO:0000269|PubMed:16844780};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: Expressed in presence of xylan and repressed by
CC       glucose. {ECO:0000269|PubMed:8917072}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBF85620.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA64983.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; Z49894; CAA90075.1; -; Genomic_DNA.
DR   EMBL; DQ490475; ABF50851.1; -; mRNA.
DR   EMBL; AACD01000029; EAA64983.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF85620.1; ALT_SEQ; Genomic_DNA.
DR   PIR; JC5034; JC5034.
DR   RefSeq; XP_659422.1; XM_654330.1.
DR   PDB; 1TA3; X-ray; 1.70 A; B=25-327.
DR   PDBsum; 1TA3; -.
DR   ProteinModelPortal; Q00177; -.
DR   SMR; Q00177; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   PRIDE; Q00177; -.
DR   EnsemblFungi; EAA64983; EAA64983; AN1818.2.
DR   GeneID; 2874673; -.
DR   KEGG; ani:AN1818.2; -.
DR   HOGENOM; HOG000019847; -.
DR   InParanoid; Q00177; -.
DR   KO; K01181; -.
DR   OrthoDB; EOG092C45ID; -.
DR   BRENDA; 3.2.1.8; 517.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; Q00177; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Complete proteome;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     24       {ECO:0000250}.
FT   CHAIN        25    327       Endo-1,4-beta-xylanase C.
FT                                /FTId=PRO_0000007974.
FT   DOMAIN       44    325       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   ACT_SITE    154    154       Proton donor. {ECO:0000250}.
FT   ACT_SITE    262    262       Nucleophile. {ECO:0000250}.
FT   MOD_RES      25     25       Pyrrolidone carboxylic acid.
FT                                {ECO:0000250}.
FT   DISULFID    280    286       {ECO:0000269|PubMed:15181003}.
FT   HELIX        29     35       {ECO:0000244|PDB:1TA3}.
FT   STRAND       39     45       {ECO:0000244|PDB:1TA3}.
FT   HELIX        47     51       {ECO:0000244|PDB:1TA3}.
FT   HELIX        53     62       {ECO:0000244|PDB:1TA3}.
FT   STRAND       64     70       {ECO:0000244|PDB:1TA3}.
FT   HELIX        74     77       {ECO:0000244|PDB:1TA3}.
FT   HELIX        87     98       {ECO:0000244|PDB:1TA3}.
FT   STRAND      102    109       {ECO:0000244|PDB:1TA3}.
FT   STRAND      111    113       {ECO:0000244|PDB:1TA3}.
FT   HELIX       116    119       {ECO:0000244|PDB:1TA3}.
FT   HELIX       124    141       {ECO:0000244|PDB:1TA3}.
FT   TURN        142    144       {ECO:0000244|PDB:1TA3}.
FT   STRAND      147    154       {ECO:0000244|PDB:1TA3}.
FT   STRAND      160    162       {ECO:0000244|PDB:1TA3}.
FT   HELIX       166    171       {ECO:0000244|PDB:1TA3}.
FT   HELIX       174    186       {ECO:0000244|PDB:1TA3}.
FT   STRAND      190    197       {ECO:0000244|PDB:1TA3}.
FT   HELIX       205    219       {ECO:0000244|PDB:1TA3}.
FT   STRAND      226    229       {ECO:0000244|PDB:1TA3}.
FT   HELIX       240    242       {ECO:0000244|PDB:1TA3}.
FT   HELIX       243    251       {ECO:0000244|PDB:1TA3}.
FT   STRAND      256    265       {ECO:0000244|PDB:1TA3}.
FT   HELIX       270    281       {ECO:0000244|PDB:1TA3}.
FT   STRAND      286    292       {ECO:0000244|PDB:1TA3}.
FT   HELIX       296    298       {ECO:0000244|PDB:1TA3}.
FT   HELIX       302    304       {ECO:0000244|PDB:1TA3}.
FT   STRAND      307    309       {ECO:0000244|PDB:1TA3}.
FT   HELIX       317    326       {ECO:0000244|PDB:1TA3}.
SQ   SEQUENCE   327 AA;  35441 MW;  B59CF4DE435F6F20 CRC64;
     MVHLKTLAGS AVFASLATAA VLPRQSASLN DLFVAAGKSY FGTCSDQALL QNSQNEAIVA
     SQFGVITPEN SMKWDALEPS QGNFGWSGAD YLVDYATQHN KKVRGHTLVW HSQLPSWVSS
     IGDANTLRSV MTNHINEVVG RYKGKIMHWD VVNEIFNEDG TFRNSVFYNL LGEDFVRIAF
     ETARAADPDA KLYINDYNLD SASYAKTQAM ASYVKKWLAE GVPIDGIGSQ AHYSSSHWSS
     TEAAGALSSL ANTGVSEVAI TELDIAGAAS SDYLNLLNAC LNEQKCVGIT VWGVSDKDSW
     RASDSPLLFD GNYQPKDAYN AIVNALS
//
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