ID   XYNF3_ASPOR             Reviewed;         323 AA.
AC   Q96VB6; Q2UNW4;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   22-FEB-2023, entry version 94.
DE   RecName: Full=Endo-1,4-beta-xylanase F3;
DE            Short=Xylanase F3;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase F3;
DE   Flags: Precursor;
GN   Name=xynF3; Synonyms=xlnF3; ORFNames=AO090001000208;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11999400; DOI=10.1271/bbb.66.285;
RA   Kimura T., Suzuki H., Furuhashi H., Aburatani T., Morimoto K., Sakka K.,
RA   Ohmiya K.;
RT   "Molecular cloning, characterization, and expression analysis of the xynF3
RT   gene from Aspergillus oryzae.";
RL   Biosci. Biotechnol. Biochem. 66:285-292(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VTCC-F-187;
RA   Quyen D.T., Nguyen S.L.T.;
RT   "Gene cloning, sequencing, expression and characterization of a xylanase
RT   gene from Aspergillus niger DMS1957.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=16672490; DOI=10.1128/aem.72.5.3448-3457.2006;
RA   Oda K., Kakizono D., Yamada O., Iefuji H., Akita O., Iwashita K.;
RT   "Proteomic analysis of extracellular proteins from Aspergillus oryzae grown
RT   under submerged and solid-state culture conditions.";
RL   Appl. Environ. Microbiol. 72:3448-3457(2006).
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:11999400}.
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       Kinetic parameters:
CC         KM=200 uM for birch wood xylan {ECO:0000269|PubMed:11999400};
CC         Vmax=435 umol/min/mg enzyme {ECO:0000269|PubMed:11999400};
CC       pH dependence:
CC         Optimum pH is 5.5. Retain 85 percent of its activity in the pH range
CC         from 6.0 to 7.0 after a 12 h incubation at 25 degrees Celsius.
CC         {ECO:0000269|PubMed:11999400};
CC       Temperature dependence:
CC         Optimum temperature is 58 degrees Celsius. The purified enzyme showed
CC         complete stability under 60 degrees Celsius.
CC         {ECO:0000269|PubMed:11999400};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11999400,
CC       ECO:0000269|PubMed:16672490}.
CC   -!- MISCELLANEOUS: The promoter does not contain any 5'-GGCTAAA-3' sequence
CC       identified as binding sites for the xylanolytic transcriptional
CC       activator xlnR.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE56751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU848306; ACJ26383.1; -; mRNA.
DR   EMBL; AB066176; BAB69073.1; -; Genomic_DNA.
DR   EMBL; AP007154; BAE56751.1; ALT_SEQ; Genomic_DNA.
DR   PIR; JC7813; JC7813.
DR   AlphaFoldDB; Q96VB6; -.
DR   SMR; Q96VB6; -.
DR   STRING; 510516.Q96VB6; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10C_ASPOR; -.
DR   OrthoDB; 548101at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF76; ENDO-1,4-BETA-XYLANASE C; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..323
FT                   /note="Endo-1,4-beta-xylanase F3"
FT                   /id="PRO_0000393192"
FT   DOMAIN          43..322
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        153
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        259
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        277..283
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  34696 MW;  474B2F7E130AD465 CRC64;
     MVHLKSLAGI LLYTSLCIAS SQQAPASINN AFVAKGKKYF GTCADQGTLS DGTNSGIIKA
     DFGQLTPENS MKWDATEPSQ GKFSFSGADY LVNYAATNNK LIRGHTLVWH SQLPSWVQGI
     TDKNTLTSVL KNHITTVMNR YKGKVYAWDV VNEIFNEDGT LRSSVFYNVL GEDFVRIAFE
     TARAADPQAK LYINDYNLDS ANYGKTTGLA NHVKKWIAQG IPIDGIGSQT HLSAGGSSGV
     KGALNTLAAS GVSEVAITEL DIAGASSNDY VNVVEACLEV SKCVGITVWG VSDKNSWRSA
     ESPLLFDGNY QPKSAYNAIL NAL
//