XYNA_ASPOR
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 03-AUG-2022, entry version 112.
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;
OC Aspergillus subgen. Circumdati.
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., Karita S.,
RA Sakka K., Ohmiya K.;
RT "Molecular cloning, overexpression, and purification of a major xylanase
RT 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., 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:11210150}.
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=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 range
CC from 5.0 to 7.0, and 70 percent activity in the pH range from 4.0 to
CC 8.0. {ECO:0000269|PubMed:11210150};
CC Temperature dependence:
CC Optimum temperature is 58 degrees Celsius. Has complete stability at
CC 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) family.
CC {ECO:0000305}.
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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 AlphaFoldDB; Q9HFA4; -.
DR SMR; Q9HFA4; -.
DR STRING; 510516.Q9HFA4; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_ASPOR; -.
DR EnsemblFungi; BAE62665; BAE62665; AO090120000026.
DR GeneID; 5996057; -.
DR KEGG; aor:AO090120000026; -.
DR VEuPathDB; FungiDB:AO090120000026; -.
DR HOGENOM; CLU_052631_0_0_1; -.
DR OMA; DYWQNWT; -.
DR BioCyc; MetaCyc:MON-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; Direct protein sequencing; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..232
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000393162"
FT DOMAIN 44..232
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 128
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="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
