XYLA_ASPNC
ID XYLA_ASPNC Reviewed; 736 AA.
AC A2QTU5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Alpha-xylosidase A {ECO:0000303|PubMed:22033931};
DE EC=3.2.1.177 {ECO:0000269|PubMed:22033931};
DE Flags: Precursor;
GN Name=axlA {ECO:0000303|PubMed:22033931}; ORFNames=An09g03300;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22033931; DOI=10.1074/jbc.m111.307397;
RA Scott-Craig J.S., Borrusch M.S., Banerjee G., Harvey C.M., Walton J.D.;
RT "Biochemical and molecular characterization of secreted alpha-xylosidase
RT from Aspergillus niger.";
RL J. Biol. Chem. 286:42848-42854(2011).
CC -!- FUNCTION: Catalyzes the liberation of alpha-xylose from the non-
CC reducing terminal glucose of xyloglucan oligosaccharides.
CC {ECO:0000269|PubMed:22033931}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-xylose residues
CC with release of alpha-D-xylose.; EC=3.2.1.177;
CC Evidence={ECO:0000269|PubMed:22033931};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.68 mM for isoprimeverose {ECO:0000269|PubMed:22033931};
CC KM=9.78 mM for pNP-alpha-D-xyloside {ECO:0000269|PubMed:22033931};
CC pH dependence:
CC Optimum pH is 3.0-4.0. {ECO:0000269|PubMed:22033931};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:22033931};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22033931}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; AM270197; CAK40270.1; -; Genomic_DNA.
DR RefSeq; XP_001393647.1; XM_001393610.1.
DR PDB; 6DRU; X-ray; 2.70 A; A/B=19-736.
DR PDBsum; 6DRU; -.
DR AlphaFoldDB; A2QTU5; -.
DR SMR; A2QTU5; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR CLAE; AXL31A_ASPNG; -.
DR PaxDb; A2QTU5; -.
DR PRIDE; A2QTU5; -.
DR EnsemblFungi; CAK40270; CAK40270; An09g03300.
DR GeneID; 4983866; -.
DR KEGG; ang:ANI_1_1306084; -.
DR VEuPathDB; FungiDB:An09g03300; -.
DR HOGENOM; CLU_000631_7_3_1; -.
DR Proteomes; UP000006706; Chromosome 1L.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0016020; C:membrane; IDA:AspGD.
DR GO; GO:0061634; F:alpha-D-xyloside xylohydrolase; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:AspGD.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..736
FT /note="Alpha-xylosidase A"
FT /evidence="ECO:0000255"
FT /id="PRO_5000220438"
FT ACT_SITE 413
FT /evidence="ECO:0000250|UniProtKB:P31434"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31434"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:6DRU"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 221..232
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 280..292
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:6DRU"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 388..401
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 416..426
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 431..435
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 457..473
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 510..526
FT /evidence="ECO:0007829|PDB:6DRU"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 553..566
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 569..574
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:6DRU"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 600..612
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 614..627
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:6DRU"
FT TURN 640..642
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 646..651
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:6DRU"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 678..684
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:6DRU"
FT TURN 698..700
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 706..713
FT /evidence="ECO:0007829|PDB:6DRU"
FT STRAND 721..725
FT /evidence="ECO:0007829|PDB:6DRU"
FT HELIX 727..730
FT /evidence="ECO:0007829|PDB:6DRU"
SQ SEQUENCE 736 AA; 82593 MW; 0AA2256B6288F48A CRC64;
MYFSSFLALG ALVQAAAATY FAPNSTGLRI QHGFETILIQ PFGYDGFRVR AWPFRPPSGN
EISFIYDPPI EGYEDTAHGM SYDTATTGTE PRTLRNGNII LRTTGWGGTT AGYRLSFYRV
NDDGSETLLT NEYAPLKSLN PRYYYWPGPG AEFSAEFSFS ATPDEQIYGT GTQQDHMINK
KGSVIDMVNF NSYIPTPVFM SNKGYAFIWN MPAEGRMEFG TLRTRFTAAS TTLVDYVIVA
AQPGDYDTLQ QRISALTGRA PAPPDFSLGY IQSKLRYENQ TEVELLAQNF HDRNIPVSMI
VIDYQSWAHQ GDWALDPRLW PNVAQMSARV KNLTGAEMMA SLWPSVADDS VNYAALQANG
LLSATRDGPG TTDSWNGSYI RNYDSTNPSA RKFLWSMLKK NYYDKGIKNF WIDQADGGAL
GEAYENNGQS TYIESIPFTL PNVNYAAGTQ LSVGKLYPWA HQQAIEEGFR NATDTKEGSA
CDHVSLSRSG YIGSQRFCSM IWSGDTTSVW DTLAVQVASG LSAAATGWGW WTVDAGGFEV
DSTVWWSGNI DTPEYRELYV RWLAWTTFLP FMRTHGSRTC YFQDAYTCAN EPWSYGASNT
PIIVSYIHLR YQLGAYLKSI FNQFHLTGRS IMRPLYMDFE KTDPKISQLV SSNSNYTTQQ
YMFGPRLLVS PVTLPNVTEW PVYLPQTGQN NTKPWTYWWT NETYAGGQVV KVPAPLQHIP
VFHLGSREEL LSGNVF
