LXR4_HYPJQ
ID LXR4_HYPJQ Reviewed; 304 AA.
AC G0RNA2;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=L-xylo-3-hexulose reductase {ECO:0000303|PubMed:22654107};
DE EC=1.1.1.- {ECO:0000269|PubMed:22654107};
GN Name=lxr4 {ECO:0000303|PubMed:22654107}; ORFNames=TRIREDRAFT_22771;
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, INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
CC -!- FUNCTION: L-xylulose reductase involved in the catabolism of D-
CC galactose through an oxidoreductive pathway. Catalyzes the NADPH-
CC dependent reduction of L-xylo-3-hexulose. Is also active with D-
CC ribulose and L-xylulose, and to a lesser extent with D-xylulose, D-
CC fructose and L- and D-sorbose. In the reverse reaction, shows activity
CC with D-sorbitol and D-mannitol, low activity with xylitol, but no
CC activity with galactitol, ribitol, and L- and D-arabitol.
CC {ECO:0000269|PubMed:22654107}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sorbitol + NADP(+) = H(+) + L-xylo-3-hexulose + NADPH;
CC Xref=Rhea:RHEA:51552, ChEBI:CHEBI:15378, ChEBI:CHEBI:17924,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:134214;
CC Evidence={ECO:0000269|PubMed:22654107};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 mM for L-xylo-3-hexulose {ECO:0000269|PubMed:22654107};
CC KM=47 mM for D-ribulose {ECO:0000269|PubMed:22654107};
CC KM=22 mM for L-xylulose {ECO:0000269|PubMed:22654107};
CC Vmax=5.5 umol/min/mg enzyme towards L-xylo-3-hexulose
CC {ECO:0000269|PubMed:22654107};
CC Vmax=14 umol/min/mg enzyme towards D-ribulose
CC {ECO:0000269|PubMed:22654107};
CC Vmax=4.2 umol/min/mg enzyme towards L-xylulose
CC {ECO:0000269|PubMed:22654107};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Decreases growth on D-galactose and impairs
CC growth on galactitol. {ECO:0000269|PubMed:22654107}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL985069; EGR47347.1; -; Genomic_DNA.
DR EMBL; BK008566; DAA35179.1; -; Genomic_DNA.
DR RefSeq; XP_006966715.1; XM_006966653.1.
DR AlphaFoldDB; G0RNA2; -.
DR SMR; G0RNA2; -.
DR STRING; 51453.EGR47347; -.
DR EnsemblFungi; EGR47347; EGR47347; TRIREDRAFT_22771.
DR GeneID; 18484185; -.
DR KEGG; tre:TRIREDRAFT_22771; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_22771; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR BioCyc; MetaCyc:MON-18677; -.
DR SABIO-RK; G0RNA2; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
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 Carbohydrate metabolism; Galactose metabolism; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..304
FT /note="L-xylo-3-hexulose reductase"
FT /id="PRO_0000433647"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 15..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 165..201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
SQ SEQUENCE 304 AA; 32296 MW; FDE2F57AA326ACAA CRC64;
MARPYEGKLA IVTGASRGIG AAVARRLAAK GSNVLITFTS DSSRDLTRGL VEELSSKHGV
HVQSVQTDLA KASTAAPIIV EAARTLFDSY SPPSGGKKFQ VDILINNAGV SSNQFLNDPE
KGAIDEAEFT RVYAINVLAP LLLTQAVAPH LPADRSGRIV NVSSVSASIG YLGQSVYAGS
KGALEVMTRT WARELAERAT VNSVNPGPAW GDMYAEAGPT FWRRNQPYVD AAPLMAYDGE
EDVLRRAGGE ADKFDRLVRE QMGGRRPGFA DEIAGTVDML CTEESGWTTG SVVCANGGMR
MSIA
