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Database: UniProt
Entry: Q9HFA4
LinkDB: Q9HFA4
Original site: Q9HFA4 
ID   XYNA_ASPOR              Reviewed;         232 AA.
AC   Q9HFA4;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   10-APR-2019, entry version 100.
DE   RecName: Full=Endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE   AltName: Full=Endo-1,4-beta-xylanase G2;
DE            Short=Xylanase G2;
DE   Flags: Precursor;
GN   Name=xlnA; Synonyms=xlnG2, xynG2; ORFNames=AO090120000026;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-64, FUNCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11210150; DOI=10.1271/bbb.64.2734;
RA   Kimura T., Suzuki H., Furuhashi H., Aburatani T., Morimoto K.,
RA   Karita S., Sakka K., Ohmiya K.;
RT   "Molecular cloning, overexpression, and purification of a major
RT   xylanase from Aspergillus oryzae.";
RL   Biosci. Biotechnol. Biochem. 64:2734-2738(2000).
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 beta-
RT   xylanase gene from Aspergillus oryzae VTCC-F187.";
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.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., 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
RT   grown 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
CC       xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide
CC       in the biosphere, after cellulose. {ECO:0000269|PubMed:11210150}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=242.8 uM for birch wood xylan {ECO:0000269|PubMed:11210150};
CC         Vmax=123 umol/min/mg enzyme {ECO:0000269|PubMed:11210150};
CC       pH dependence:
CC         Optimum pH is 6.0. Retains over 95 percent activity in the pH
CC         range from 5.0 to 7.0, and 70 percent activity in the pH range
CC         from 4.0 to 8.0. {ECO:0000269|PubMed:11210150};
CC       Temperature dependence:
CC         Optimum temperature is 58 degrees Celsius. Has complete
CC         stability at 60 degrees Celsius. {ECO:0000269|PubMed:11210150};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16672490}.
CC   -!- MISCELLANEOUS: The promoter contains two 5'-GGCTAAA-3' sequences
CC       identified as binding sites for the xylanolytic transcriptional
CC       activator xlnR.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; EU848307; ACJ26384.1; -; mRNA.
DR   EMBL; AB044941; BAB20794.1; -; Genomic_DNA.
DR   EMBL; AP007166; BAE62665.1; -; Genomic_DNA.
DR   PIR; JC7577; JC7577.
DR   RefSeq; XP_001823798.1; XM_001823746.2.
DR   ProteinModelPortal; Q9HFA4; -.
DR   SMR; Q9HFA4; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11A_ASPOR; -.
DR   EnsemblFungi; BAE62665; BAE62665; AO090120000026.
DR   GeneID; 5996057; -.
DR   KEGG; aor:AO090120000026; -.
DR   HOGENOM; HOG000179135; -.
DR   KO; K01181; -.
DR   OMA; NMQNHFN; -.
DR   BioCyc; MetaCyc:MONOMER-16226; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006564; Chromosome 5.
DR   GO; GO:0005576; C:extracellular region; IDA:AspGD.
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; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    232       Endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000393162.
FT   DOMAIN       44    232       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    128    128       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    219    219       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   CARBOHYD     34     34       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   232 AA;  24605 MW;  1F73104751EA561C CRC64;
     MVSFSSILLA CSAAIGALAT PIEPLADHPN EAFNETAFND LVGRSTPSST GYNNGYYYSF
     WTDGGGDVTY TNGNGGSYSV QWSNVGNFVG GKGWNPGSSR AITYSGSFNP SGNGYLAVYG
     WTTDPLIEYY IVESYGTYNP GSGGTYKGQV TSDGGTYNIY TSVRTNAPSI IGTATFTQFW
     SVRTSKRVGG TVTTGNHFNA WAKYGLTLGT HNYQIVATEG YQSSGSSAIT VY
//
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