BXLB_EMENI
ID BXLB_EMENI Reviewed; 763 AA.
AC Q5ATH9; C8VEA1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Exo-1,4-beta-xylosidase bxlB;
DE EC=3.2.1.37;
DE AltName: Full=1,4-beta-D-xylan xylohydrolase bxlB;
DE AltName: Full=Beta-xylosidase bxlB;
DE AltName: Full=Xylobiase bxlB;
DE Flags: Precursor;
GN Name=bxlB; ORFNames=AN8401;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
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. Active against rye arabinoxylan and
CC xylohexaose, but not paranitrophenyl-beta-xyloside.
CC {ECO:0000269|PubMed:16844780}.
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 4.4. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 48 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; AACD01000153; EAA67023.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF80465.1; -; Genomic_DNA.
DR RefSeq; XP_681670.1; XM_676578.1.
DR AlphaFoldDB; Q5ATH9; -.
DR SMR; Q5ATH9; -.
DR STRING; 162425.CADANIAP00002874; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR CLAE; XYL3B_EMENI; -.
DR PRIDE; Q5ATH9; -.
DR EnsemblFungi; CBF80465; CBF80465; ANIA_08401.
DR EnsemblFungi; EAA67023; EAA67023; AN8401.2.
DR GeneID; 2868685; -.
DR KEGG; ani:AN8401.2; -.
DR VEuPathDB; FungiDB:AN8401; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_3_1; -.
DR InParanoid; Q5ATH9; -.
DR OMA; DKVAMTD; -.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IDA:UniProtKB.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IDA:UniProtKB.
DR GO; GO:0042285; F:xylosyltransferase activity; IDA:AspGD.
DR GO; GO:0031222; P:arabinan catabolic process; IBA:GO_Central.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR GO; GO:0045491; P:xylan metabolic 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; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..763
FT /note="Exo-1,4-beta-xylosidase bxlB"
FT /id="PRO_0000394091"
FT ACT_SITE 288
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 763 AA; 82200 MW; 6355A9F11A346F17 CRC64;
MAVFKSWNLA LLSSLFIPAL CQSNYPDCTT GPLSELPICD TSLSPLERAK SLVSALTLEE
KINNTGHEAA GSSRLGLPAY NWWNEALHGV AEKHGVSFEE SGDFSYATSF PAPIVLGAAF
NDALIRRVAE IISTEARAFS NSDHAGIDYW TPNVNPFKDP RWGRGQETPG EDPLHCSRYV
KEFVGGLQGD DPEKPKVVAT CKHLAAYDLE EWGGVSRFEF DAKVSAVDLL EYYLPPFKTC
AVDASVGAFM CSYNALNGVP ACADRYLLQT VLREHWGWEG PGHWVTGDCG AVERIQTYHH
YVESGPEAAA AALNAGVDLD CGTWLPSYLG EAERQGLISN ETLDAALTRL YTSLVQLGYF
DPAEGQPLRS LGWDDVATSE AEELAKTVAI QGTVLLKNID WTLPLKANGT LALIGPFINF
TTELQSNYAG PAKHIPTMIE AAERLGYNVL TAPGTEVNST STDGFDDALA IAAEADALIF
FGGIDNTVEE ESLDRTRIDW PGNQEELILE LAELGRPLTV VQFGGGQVDD SALLASAGVG
AIVWAGYPSQ AGGAGVFDVL TGKAAPAGRL PITQYPKSYV DEVPMTDMNL QPGTDNPGRT
YRWYEDAVLP FGFGLHYTTF NVSWAKKAFG PYDAATLARG KNPSSNIVDT FSLAVTNTGD
VASDYVALVF ASAPELGAQP APIKTLVGYS RASLIKPGET RKVDVEVTVA PLTRATEDGR
VVLYPGEYTL LVDVNDEYPT AKFEIKGDVQ VLEKFPLSGN DSD
