XYNC_ASPFU
ID XYNC_ASPFU Reviewed; 325 AA.
AC Q0H904; A3FG82; Q4WPJ5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 72.
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 Flags: Precursor;
GN Name=xlnC; Synonyms=xynf10a;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SL1;
RA Dabrowski S., Ahring B.K.;
RT "Characterization of recombinant xylan degrading enzymes from Aspergillus
RT fumigatus isolate SL1.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MKU1;
RA Thiagarajan S., Jeya M., Gunasekaran P.;
RT "Cloning and characterization of xynf10a gene from Aspergillus fumigatus
RT MKU1.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Expressed in presence of xylan and repressed by glucose.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL89839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ156555; ABA40421.1; -; mRNA.
DR EMBL; EF375874; ABN48479.1; -; Genomic_DNA.
DR EMBL; AAHF01000005; EAL89839.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_751877.1; XM_746784.1.
DR AlphaFoldDB; Q0H904; -.
DR SMR; Q0H904; -.
DR STRING; 746128.CADAFUBP00006482; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR GeneID; 3509139; -.
DR KEGG; afm:AFUA_4G09480; -.
DR InParanoid; Q0H904; -.
DR OrthoDB; 829814at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; ISS:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; ISS: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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..325
FT /note="Endo-1,4-beta-xylanase C"
FT /id="PRO_0000393188"
FT DOMAIN 44..324
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 155
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 261
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT DISULFID 279..285
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="V -> A (in Ref. 1; ABA40421)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="K -> R (in Ref. 1; ABA40421)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="Y -> C (in Ref. 1; ABA40421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 35221 MW; BB2D1688371B3F92 CRC64;
MVVLSKLVSS ILFVSLVSAG VIEERQAASI NQAFTSHGKK YFGTASDQAL LQKSQNEAIV
RKDFGQLTPE NSMKWDATEP SQGRFNFAGA DFLVNYAKQN GKKVRGHTLV WHSQLPSWVS
AISDKNTLTS VLKNHITTVM TRYKGQIYAW DVVNEIFNED GSLRDSVFSR VLGEDFVRIA
FETARSVDPS AKLYINDYNL DSASYGKTQG MVRYVKKWLA AGIPIDGIGT QTHLGAGASS
SVKGALTALA SSGVSEVAIT ELDIAGASSQ DYVNVVKACL DVPKCVGITV WGVSDRDSWR
SGSSPLLFDS NYQPKAAYNA IIAAL
