XYL1_EMENI
ID XYL1_EMENI Reviewed; 319 AA.
AC Q5BGA7; C8VTG2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable NAD(P)H-dependent D-xylose reductase xyl1;
DE Short=XR;
DE EC=1.1.1.307;
GN Name=xyl1; ORFNames=AN0423;
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).
CC -!- FUNCTION: Catalyzes the initial reaction in the xylose utilization
CC pathway by reducing D-xylose into xylitol. Xylose is a major component
CC of hemicelluloses such as xylan. Most fungi utilize D-xylose via three
CC enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase
CC (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters
CC pentose phosphate pathway (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + xylitol = D-xylose + H(+) + NADH;
CC Xref=Rhea:RHEA:27441, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC ChEBI:CHEBI:53455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.307;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + xylitol = D-xylose + H(+) + NADPH;
CC Xref=Rhea:RHEA:27445, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.307;
CC -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AACD01000007; EAA66522.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF89516.1; -; Genomic_DNA.
DR RefSeq; XP_658027.1; XM_652935.1.
DR AlphaFoldDB; Q5BGA7; -.
DR SMR; Q5BGA7; -.
DR STRING; 162425.CADANIAP00002275; -.
DR EnsemblFungi; CBF89516; CBF89516; ANIA_00423.
DR EnsemblFungi; EAA66522; EAA66522; AN0423.2.
DR GeneID; 2876201; -.
DR KEGG; ani:AN0423.2; -.
DR VEuPathDB; FungiDB:AN0423; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; Q5BGA7; -.
DR OMA; AFKPGNE; -.
DR OrthoDB; 1016440at2759; -.
DR UniPathway; UPA00810; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0032866; F:D-xylose:NADP reductase activity; IEA:InterPro.
DR GO; GO:0042843; P:D-xylose catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd19115; AKR_AKR2D1; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044487; AKR2D.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome;
KW Xylose metabolism.
FT CHAIN 1..319
FT /note="Probable NAD(P)H-dependent D-xylose reductase xyl1"
FT /id="PRO_0000393503"
FT ACT_SITE 50
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166..167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 215..224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 271..281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 79
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 319 AA; 35604 MW; 038CE5EF3FC51911 CRC64;
MSPPTVKLNS GYDMPLVGFG LWKVNNDTCA DQVYEAIKAG YRLFDGACDY GNEVEAGQGV
ARAIKEGIVK RSDLFIVSKL WNSFHDGERV EPIARKQLSD WGIDYFDLYI VHFPVSLKYV
DPEVRYPPGW ENAEGKVELG KATIQETWTA MESLVDKGLA RSIGISNFSA QLLLDLLRYA
RIRPATLQIE HHPYLTQERL VTFAQREGIA VTAYSSFGPL SFLELSVKQA EGAPPLFEHP
VIKDIAEKHG KTPAQVLLRW ATQRGIAVIP KSNNPARLLQ NLDVVGFDLE DGELKAISDL
DKGLRFNDPP NYGLPITIF
