ID   XYNF1_ASPOR             Reviewed;         327 AA.
AC   O94163; Q2TY21;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   22-FEB-2023, entry version 91.
DE   RecName: Full=Endo-1,4-beta-xylanase F1;
DE            Short=Xylanase F1;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase F1;
DE   Flags: Precursor;
GN   Name=xynF1; Synonyms=xlnF1; ORFNames=AO090103000423;
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 [GENOMIC DNA].
RC   STRAIN=KBN616;
RX   PubMed=9866173; DOI=10.1007/s002530051334;
RA   Kitamoto N., Yoshino S., Ito M., Kimura T., Ohmiya K., Tsukagoshi N.;
RT   "Repression of the expression of genes encoding xylanolytic enzymes in
RT   Aspergillus oryzae by introduction of multiple copies of the xynF1
RT   promoter.";
RL   Appl. Microbiol. Biotechnol. 50:558-563(1998).
RN   [2]
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   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10586505; DOI=10.1271/bbb.63.1791;
RA   Kitamoto N., Yoshino S., Ohmiya K., Tsukagoshi N.;
RT   "Purification and characterization of the overexpressed Aspergillus oryzae
RT   xylanase, XynF1.";
RL   Biosci. Biotechnol. Biochem. 63:1791-1794(1999).
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:10586505}.
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 5.0. {ECO:0000269|PubMed:10586505};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:10586505};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10586505}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE65852.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB011212; BAA75475.1; -; Genomic_DNA.
DR   EMBL; AP007174; BAE65852.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; O94163; -.
DR   SMR; O94163; -.
DR   STRING; 510516.O94163; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10F_ASPOR; -.
DR   OrthoDB; 548101at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006564; Chromosome 8.
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   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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..327
FT                   /note="Endo-1,4-beta-xylanase F1"
FT                   /id="PRO_0000393191"
FT   DOMAIN          45..326
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        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        281..287
FT                   /evidence="ECO:0000250"
FT   CONFLICT        190
FT                   /note="N -> D (in Ref. 2; BAE65852)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="K -> Q (in Ref. 2; BAE65852)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   327 AA;  35402 MW;  38B2F6374BAD3D0A CRC64;
     MVHLKALASG TLFASLASSA VISRQAAASI NDAFVAHGKK YFGTCSDQAL LQNSQNEAIV
     RADFGQLTPE NSMKWDALEP SQGSFSFAGA DFLADYAKTN NKLVRGHTLV WHSQLPSWVQ
     GITDKDTLTE VIKNHITTIM QRYKGQIYAW DVVNEIFDED GTLRDSVFSQ VLGEDFVRIA
     FETAREADPN AKLYINDYNL DSADYAKTKG MVSYVKKWLD AGVPIDGIGS QSHYSANGFP
     VSGAKGALTA LASTGVSEVA VTELDIEGAS SESYLEVVNA CLDVSSCVGI TVWGVSDKDS
     WRSSTSPLLF DSNYQAKDAY NAIIDAL
//