XYNC_EMENI
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 25-MAY-2022, entry version 135.
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 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
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., Ramon D.;
RT "Identification, isolation and sequence of the Aspergillus nidulans xlnC
RT gene encoding the 34-kDa xylanase.";
RL Gene 175:29-33(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL 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 enzymes
RT 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., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., 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., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=25043916; DOI=10.1186/1471-2164-15-613;
RA Martins I., Hartmann D.O., Alves P.C., Martins C., Garcia H.,
RA Leclercq C.C., Ferreira R., He J., Renaut J., Becker J.D.,
RA Silva Pereira C.;
RT "Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant
RT polyester suberin as carbon source.";
RL BMC Genomics 15:613-613(2014).
RN [6]
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: structural
RT basis for the inhibition of family 10 and family 11 xylanases.";
RL J. Biol. Chem. 279:36029-36037(2004).
CC -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose. {ECO:0000269|PubMed:16844780,
CC ECO:0000269|PubMed:8917072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
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 {ECO:0000269|PubMed:25043916}.
CC -!- INDUCTION: Expressed in presence of xylan and repressed by glucose.
CC {ECO:0000269|PubMed:8917072}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {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};
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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 AlphaFoldDB; Q00177; -.
DR SMR; Q00177; -.
DR STRING; 162425.CADANIAP00008467; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR EnsemblFungi; EAA64983; EAA64983; AN1818.2.
DR GeneID; 2874673; -.
DR KEGG; ani:AN1818.2; -.
DR eggNOG; ENOG502QSCW; Eukaryota.
DR HOGENOM; CLU_020161_2_0_1; -.
DR InParanoid; Q00177; -.
DR OrthoDB; 829814at2759; -.
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; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
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; Disulfide bond; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..327
FT /note="Endo-1,4-beta-xylanase C"
FT /id="PRO_0000007974"
FT DOMAIN 44..325
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 154
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 280..286
FT /evidence="ECO:0000269|PubMed:15181003"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:1TA3"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 317..326
FT /evidence="ECO:0007829|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
