LXR3_HYPJQ
ID LXR3_HYPJQ Reviewed; 288 AA.
AC G0RH19;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=L-xylulose reductase {ECO:0000303|PubMed:22654107};
DE EC=1.1.1.10 {ECO:0000269|PubMed:23506391};
GN Name=lxr3 {ECO:0000303|PubMed:22654107}; ORFNames=TRIREDRAFT_60033;
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a;
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
RN [2]
RP IDENTIFICATION.
RC STRAIN=QM6a;
RX PubMed=22654107; DOI=10.1074/jbc.m112.372755;
RA Mojzita D., Herold S., Metz B., Seiboth B., Richard P.;
RT "L-xylo-3-hexulose reductase is the missing link in the oxidoreductive
RT pathway for D-galactose catabolism in filamentous fungi.";
RL J. Biol. Chem. 287:26010-26018(2012).
RN [3]
RP INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23506391; DOI=10.1021/bi301583u;
RA Metz B., Mojzita D., Herold S., Kubicek C.P., Richard P., Seiboth B.;
RT "A novel L-xylulose reductase essential for L-arabinose catabolism in
RT Trichoderma reesei.";
RL Biochemistry 52:2453-2460(2013).
CC -!- FUNCTION: L-xylulose reductase involved in the catabolism of L-
CC arabinose through an oxidoreductive pathway. Catalyzes the NADPH-
CC dependent reduction of L-xylulose. Is also able to convert D-xylulose,
CC D-ribulose, L-sorbose, and D-fructose to their corresponding polyols.
CC {ECO:0000269|PubMed:23506391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + xylitol = H(+) + L-xylulose + NADPH;
CC Xref=Rhea:RHEA:17025, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC ChEBI:CHEBI:17399, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.10;
CC Evidence={ECO:0000269|PubMed:23506391};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 mM for L-xylulose {ECO:0000269|PubMed:23506391};
CC KM=0.13 mM for NADPH {ECO:0000269|PubMed:23506391};
CC KM=105 mM for D-ribulose {ECO:0000269|PubMed:23506391};
CC KM=250 mM for D-sorbitol {ECO:0000269|PubMed:23506391};
CC KM=100 mM for xylitol {ECO:0000269|PubMed:23506391};
CC Vmax=367 nmol/sec/mg enzyme towards L-xylulose
CC {ECO:0000269|PubMed:23506391};
CC Vmax=250 nmol/sec/mg enzyme towards NADPH
CC {ECO:0000269|PubMed:23506391};
CC Vmax=266 nmol/sec/mg enzyme towards D-ribulose
CC {ECO:0000269|PubMed:23506391};
CC Vmax=250 nmol/sec/mg enzyme towards D-sorbitol
CC {ECO:0000269|PubMed:23506391};
CC Vmax=100 nmol/sec/mg enzyme towards xylitol
CC {ECO:0000269|PubMed:23506391};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route):
CC step 3/5. {ECO:0000305}.
CC -!- INDUCTION: Transcription is repressed by D-glucose and induced by L-
CC arabinose and L-arabitol. {ECO:0000269|PubMed:23506391}.
CC -!- DISRUPTION PHENOTYPE: Decreases strongly levels of growth on solid
CC medium and biomass accumulation during liquid cultivation for both L-
CC arabinose and L-arabitol; and impairs L-xylulose reductase activity.
CC {ECO:0000269|PubMed:23506391}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; GL985062; EGR49477.1; -; Genomic_DNA.
DR EMBL; BK008567; DAA35180.1; -; Genomic_DNA.
DR RefSeq; XP_006964623.1; XM_006964561.1.
DR AlphaFoldDB; G0RH19; -.
DR SMR; G0RH19; -.
DR STRING; 51453.EGR49477; -.
DR EnsemblFungi; EGR49477; EGR49477; TRIREDRAFT_60033.
DR GeneID; 18486563; -.
DR KEGG; tre:TRIREDRAFT_60033; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_60033; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR BioCyc; MetaCyc:MON-18763; -.
DR SABIO-RK; G0RH19; -.
DR UniPathway; UPA00146; UER00576.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Arabinose catabolism; Carbohydrate metabolism; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..288
FT /note="L-xylulose reductase"
FT /id="PRO_0000433646"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 35..60
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 177..201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
SQ SEQUENCE 288 AA; 30564 MW; 51D6D845359C2511 CRC64;
MKNGAFPHDN AAVPNVERVL PLFSLKGRTA IVSGAGAGIG LAVAQAFAEA GANVAIWYNS
NKQAVTSAED IAKTYGVKCK AYQVNVTSAE AVDKAITEII KEFNGRLDVF VANSGITWTE
GAFIDGSVES ARNVMSVNVD GVMWCAKSAG AHFRRQKEEG TTIDGKPLDN FIAGSFIATA
SMSGSIVNVP QLQAVYNSSK AAVIHFCKSL AVEWTGFARV NTVSPGYIIT EISNFVPPET
KTLWKDKIVM GREGRVGELK GAYLYLASDA SSYTTGLDMI VDGGYSLP
