XYND_EMENI
ID XYND_EMENI Reviewed; 803 AA.
AC Q5BAS1; C8VNG4; O42810;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=xylA; ORFNames=AN2359;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=9546179; DOI=10.1128/aem.64.4.1412-1419.1998;
RA Perez-Gonzalez J.A., van Peij N.N., Bezoen A., MacCabe A.P., Ramon D.,
RA de Graaff L.H.;
RT "Molecular cloning and transcriptional regulation of the Aspergillus
RT nidulans xlnD gene encoding a beta-xylosidase.";
RL Appl. Environ. Microbiol. 64:1412-1419(1998).
RN [2]
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 [3]
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 [4]
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. {ECO:0000269|PubMed:16844780,
CC ECO:0000269|PubMed:9546179}.
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 5.1. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 52 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; Y13568; CAA73902.1; -; Genomic_DNA.
DR EMBL; AACD01000039; EAA64470.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF86686.1; -; Genomic_DNA.
DR RefSeq; XP_659963.1; XM_654871.1.
DR PDB; 6Q7I; X-ray; 1.48 A; A/B=19-803.
DR PDB; 6Q7J; X-ray; 2.14 A; A/B=20-803.
DR PDBsum; 6Q7I; -.
DR PDBsum; 6Q7J; -.
DR AlphaFoldDB; Q5BAS1; -.
DR SMR; Q5BAS1; -.
DR STRING; 162425.CADANIAP00009060; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR CLAE; XYL3C_EMENI; -.
DR EnsemblFungi; CBF86686; CBF86686; ANIA_02359.
DR EnsemblFungi; EAA64470; EAA64470; AN2359.2.
DR GeneID; 2875035; -.
DR KEGG; ani:AN2359.2; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_3_1; -.
DR InParanoid; Q5BAS1; -.
DR OMA; WATSFPM; -.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000000560; Chromosome VII.
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; IBA:GO_Central.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IDA:UniProtKB.
DR GO; GO:0031222; P:arabinan catabolic process; IBA:GO_Central.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
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 3D-structure; Carbohydrate metabolism; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal; Xylan degradation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..803
FT /note="Exo-1,4-beta-xylosidase xlnD"
FT /id="PRO_0000393293"
FT ACT_SITE 307
FT /evidence="ECO:0000250"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 14..15
FT /note="PT -> A (in Ref. 1; CAA73902)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="S -> T (in Ref. 1; CAA73902)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="G -> A (in Ref. 1; CAA73902)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="L -> S (in Ref. 1; CAA73902)"
FT /evidence="ECO:0000305"
FT CONFLICT 754..755
FT /note="EL -> DV (in Ref. 1; CAA73902)"
FT /evidence="ECO:0000305"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:6Q7I"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 141..160
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:6Q7I"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:6Q7I"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 343..353
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 359..375
FT /evidence="ECO:0007829|PDB:6Q7I"
FT TURN 376..379
FT /evidence="ECO:0007829|PDB:6Q7I"
FT TURN 385..388
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 391..398
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 402..410
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 456..462
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 483..492
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 493..501
FT /evidence="ECO:0007829|PDB:6Q7I"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 522..529
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 536..544
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 559..564
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:6Q7J"
FT HELIX 570..578
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:6Q7J"
FT HELIX 597..600
FT /evidence="ECO:0007829|PDB:6Q7I"
FT TURN 612..615
FT /evidence="ECO:0007829|PDB:6Q7I"
FT TURN 621..623
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 648..654
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 655..660
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 672..683
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 689..700
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 710..720
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 725..733
FT /evidence="ECO:0007829|PDB:6Q7I"
FT HELIX 735..737
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 746..748
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 751..757
FT /evidence="ECO:0007829|PDB:6Q7I"
FT TURN 758..761
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 762..771
FT /evidence="ECO:0007829|PDB:6Q7I"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:6Q7I"
SQ SEQUENCE 803 AA; 87196 MW; 9EF12F7391B043B2 CRC64;
MRSLISVAVL SALPTAFSQA NTSYTDYNVE ANPDLFPLCL QHLNASFPDC ASGPLSLTPV
CDRSLSPKDR ATALVSLFTF DELVNNTGNT GLGVSRLGLP NYQVWGEALH GVGRANFVES
GNFSWATSFP MPITMMAALN KTLIHQIGTI VSTQLRAFSN AGLGGVDVYS PNINTFRHPV
WGRGQETPGE DAFLTSVYGY EYITALQGGV DPETLKIIAT AKHYAGYDIE SWNNHSRLGN
DMQITQQELS EYYTPPFIVA SRDAKVRSVM CSYNAVNGVP SCANKFFLQT LLRDTFEFSE
DGYVSGDCGA VYNVWNPHGY ASNEAAASAD SILAGTDIDC GTSYQWHSED AFEDSLVSRS
DIERGVIRLY SNLVQAGYFD GEDAPYRDIT WDDVLSTDAW NIAYEAAVEG IVLLKNDETL
PLSKDIKSVA VIGPWANVTE ELQGNYFGPA PYLISPLTGF RDSGLDVHYA LGTNLTSHST
SGFEEALTAA KQADAIIFAG GIDNTIEAEA MDRENITWPG NQLDLISKLS ELGKPLVVLQ
MGGGQVDSSS LKDNDNVNAL IWGGYPGQSG GHALADIITG KRAPAGRLVT TQYPAEYAEV
FPAIDMNLRP NETSGNPGQT YMWYTGTPVY EFGHGLFYTT FEESTETTDA GSFNIQTVLT
TPHSGYEHAQ QKTLLNFTAT VKNTGERESD YTALVYVNTT AGPAPYPKKW VVGFDRLGGL
EPGDSQTLTV PVTVESVART DEQGNRVLYP GSYELALNNE RSVVVKFELK GEEAVILSWP
EDTTSDFVSS IDGGLDRKQD VIA
