AGDD_EMENI
ID AGDD_EMENI Reviewed; 780 AA.
AC Q5AW25; C8VBI7; Q1HFR5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Alpha-xylosidase {ECO:0000303|PubMed:16844780};
DE EC=3.2.1.177 {ECO:0000269|PubMed:16844780};
GN Name=agdD {ECO:0000303|PubMed:17031028}; Synonyms=axlA; ORFNames=AN7505;
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 INDUCTION.
RX PubMed=17031028; DOI=10.1271/bbb.50694;
RA Nakamura T., Maeda Y., Tanoue N., Makita T., Kato M., Kobayashi T.;
RT "Expression profile of amylolytic genes in Aspergillus nidulans.";
RL Biosci. Biotechnol. Biochem. 70:2363-2370(2006).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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: Catalyzes the liberation of alpha-xylose from the non-
CC reducing terminal glucose of xyloglucan oligosaccharides.
CC {ECO:0000269|PubMed:16844780}.
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:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16844780}.
CC -!- INDUCTION: Despite the presence of an amyR-binding consensus sequence
CC in the promoter, is not activated by isomaltose.
CC {ECO:0000269|PubMed:17031028}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; BN001304; CBF79518.1; -; Genomic_DNA.
DR EMBL; AACD01000129; EAA62085.1; -; Genomic_DNA.
DR RefSeq; XP_680774.1; XM_675682.1.
DR AlphaFoldDB; Q5AW25; -.
DR SMR; Q5AW25; -.
DR STRING; 162425.CADANIAP00000604; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR CLAE; AXL31A_EMENI; -.
DR EnsemblFungi; CBF79518; CBF79518; ANIA_07505.
DR EnsemblFungi; EAA62085; EAA62085; AN7505.2.
DR GeneID; 2869357; -.
DR KEGG; ani:AN7505.2; -.
DR VEuPathDB; FungiDB:AN7505; -.
DR eggNOG; KOG1065; Eukaryota.
DR HOGENOM; CLU_000631_10_0_1; -.
DR InParanoid; Q5AW25; -.
DR OMA; QGVDCFK; -.
DR OrthoDB; 238940at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0061634; F:alpha-D-xyloside xylohydrolase; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB.
DR GO; GO:0010411; P:xyloglucan metabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted.
FT CHAIN 1..780
FT /note="Alpha-xylosidase"
FT /id="PRO_0000432722"
FT ACT_SITE 434
FT /evidence="ECO:0000250|UniProtKB:P31434"
FT ACT_SITE 437
FT /evidence="ECO:0000250|UniProtKB:P31434"
FT ACT_SITE 501
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31434"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 780 AA; 87991 MW; 74FE33E888FE2391 CRC64;
MKFTEGMWLL REGIRIDWMS NVERLNVDKD TVNLLLNKFQ RHRGDTLNSS TVSARVTSPL
EGIIGVKLVH WAGGLDNGPH YELNTSAGHT EITHEKGKNL KYTSGRLELD INIAPNELAF
TFTTGADGQD KRKKLTGHSF RSIGYVGDST TPKSQLSDGI FYERQGYTLA ELDLSVGEKL
YGLGERFGPF VKNGQSVNIW NEDGGTSSEL AYKNIPFYIS SNGYGVFVNH PGKVSLELQS
ERTTRVNVSV EGEELEYFVI EGKNPKEILK RWTDLTGKPA LVPAWSYGLW LTTSFTTNYS
ERTVTGFLDG FKDRNLPLSV FHFDCFWMKS YQWCDFEFDA DMFPDAAGYL ARLKERGLKL
SIWINPYVGQ ASPLFEIGKR EGYFIKRIDG SVWQWDLWQA GMAVVDFTNP AACSWYTGHL
KRLMDLGIDT FKTDFAERIP FKNITYHDGS DPARMHNYYA LLYNKVVYET MTSISGKSNS
LLFARSTSVG GQKYPVHWGG DCESTYEAMA ESLRGGLSLG LAGYIFWASD IGGFEGTPPP
ALYKRWVQFG LLSSHSRLHG SSSFRVPWIY GEDCSDVLRD CVKRKISLTP YLLAEALNGH
RSGTPLMRPM FMEFPEDLNT YPLDTQYMFG SNLLVAPVFS DEGIVTFYVP RTPEEEGRKQ
WISWFDHGKK YEGGRWYTET HGFDTLPILI RPGSVTPINY KLEKPEGNPL DGLEILVNGS
IDKEVEIEIV DPETTHKVLK VMTVSERETE NGVEVIARLD GVDGNENSVK VNWVGHGVTK
