XYND_ASPOR
ID XYND_ASPOR Reviewed; 798 AA.
AC Q2UR38; O42698; O59862;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Exo-1,4-beta-xylosidase xlnD;
DE EC=3.2.1.37;
DE AltName: Full=1,4-beta-D-xylan xylohydrolase xlnD;
DE AltName: Full=Beta-xylosidase A;
DE AltName: Full=Beta-xylosidase xlnD;
DE AltName: Full=Xylobiase xlnD;
DE Flags: Precursor;
GN Name=xlnD; Synonyms=xyl-1, xylA; ORFNames=AO090005000986;
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=HL15;
RA Hashimoto T., Nakata Y., Tsuji Y., Ito K.;
RT "Xylosidase.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=KBN616;
RX PubMed=9872754; DOI=10.1128/aem.65.1.20-24.1999;
RA Kitamoto N., Yoshino S., Ohmiya K., Tsukagoshi N.;
RT "Sequence analysis, overexpression, and antisense inhibition of a beta-
RT xylosidase gene, xylA, from Aspergillus oryzae KBN616.";
RL Appl. Environ. Microbiol. 65:20-24(1999).
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).
CC -!- FUNCTION: Xylan 1,4-beta-xylosidase involved in the hydrolysis of
CC xylan, a major structural heterogeneous polysaccharide found in plant
CC biomass representing the second most abundant polysaccharide in the
CC biosphere, after cellulose. {ECO:0000269|PubMed:9872754}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.0. Stable in the wide pH range of 3.0 to 7.0.
CC {ECO:0000269|PubMed:9872754};
CC Temperature dependence:
CC Stable at temperatures of up to 45 degrees Celsius and is inactivated
CC gradually above 45 degrees Celsius. {ECO:0000269|PubMed:9872754};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; AB009972; BAA24107.1; -; Genomic_DNA.
DR EMBL; AB013851; BAA28267.1; -; Genomic_DNA.
DR EMBL; AP007151; BAE55977.1; -; Genomic_DNA.
DR RefSeq; XP_001817979.1; XM_001817927.1.
DR AlphaFoldDB; Q2UR38; -.
DR SMR; Q2UR38; -.
DR STRING; 510516.Q2UR38; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblFungi; BAE55977; BAE55977; AO090005000986.
DR GeneID; 5990515; -.
DR KEGG; aor:AO090005000986; -.
DR VEuPathDB; FungiDB:AO090005000986; -.
DR HOGENOM; CLU_004542_5_3_1; -.
DR OMA; WPKEEQL; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IDA:AspGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IDA:AspGD.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
DR InterPro; IPR002024; Bacterioferritin.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42721; PTHR42721; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..798
FT /note="Exo-1,4-beta-xylosidase xlnD"
FT /id="PRO_0000393291"
FT ACT_SITE 310
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 31
FT /note="I -> S (in Ref. 1; BAA24107)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="G -> D (in Ref. 1; BAA24107 and 2; BAA28267)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="T -> I (in Ref. 1; BAA24107 and 2; BAA28267)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="S -> G (in Ref. 1; BAA24107 and 2; BAA28267)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="L -> P (in Ref. 1; BAA24107 and 2; BAA28267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 798 AA; 86452 MW; A8BE212A0A93C5E0 CRC64;
MPGAASIVAV LAALLPTALG QANQSYVDYN IEANPDLFSE CLETGGTSFP DCESGPLSKT
LVCDTSAKPH DRAAALVSLL TFEELVNNTA NTGHGAPRIG LPAYQVWNEA LHGVAHADFS
DAGGFSWSTS FPQPISTMAA LNRTLIHQIA TIISTQGRAF MNAGRYGLDV YSPNINTFRH
PVWGRGQETP GEDAYCLAST YAYEYITGIQ GGVDANPLKL IATAKHYAGY DIENWDNHSR
LGNDMQITQQ DLAEYYTPQF LVASRDAKVH SVMCSYNAVN GVPSCSNSFF LQTLLRDTFD
FVEDGYVSGD CGAVYNVFNP HGYATNESSA AADSIRAGTD IDCGVSYPRH FQESFHDQEV
SRQDLERGVT RLYASLIRAG YFDGKTSPYR NITWSDVVST NAQNLSYEAA AQSIVLLKND
GILPLTSTSS STKTIALIGP WANATTQMLG NYYGPAPYLI SPLQAFQDSE YKITYTIGTN
TTTDPDSTSQ STALTTAKEA DLIIFAGGID NTLETEAQDR SNITWPSNQL SLITKLADLG
KPLIVLQMGG GQVDSSALKN NKNVNALIWG GYPGQSGGQA LADIITGKRA PAARLVTTQY
PAEYAEVFPA IDMNLRPNGS NPGQTYMWYT GTPVYEFGHG LFYTNFTASA SASSGTKNRT
SFNIDEVLGR PHLGYKLVEQ MPLLNFTVDV KNTGDRVSDY TAMAFVNTTA GPAPHPNKWL
VGFDRLSAVE PGSAKTMVIP VTVDSLARTD EEGNRVLYPG RYEVALNNER EVVLGFTLTG
EKAVLFKWPK EEQLIAPQ
