XYNF1_ASPOR
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 25-MAY-2022, entry version 89.
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 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 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 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
