MTDH_HYPJE
ID MTDH_HYPJE Reviewed; 266 AA.
AC Q8NK50; A0A024SLA4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=NADP-dependent mannitol dehydrogenase {ECO:0000305};
DE Short=MtDH {ECO:0000305};
DE EC=1.1.1.138 {ECO:0000269|PubMed:19303876};
DE AltName: Full=Mannitol 2-dehydrogenase [NADP(+)] {ECO:0000303|PubMed:19303876};
GN Name=lxr1 {ECO:0000303|PubMed:12009906};
GN ORFNames=M419DRAFT_121678 {ECO:0000303|Ref.2};
OS Hypocrea jecorina (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION AS A FUNGAL L-XYLULOSE
RP REDUCTASE.
RC STRAIN=ATCC 56765 / Rut C-30;
RX PubMed=12009906; DOI=10.1021/bi025529i;
RA Richard P., Putkonen M., Vaeaenaenen R., Londesborough J., Penttilae M.;
RT "The missing link in the fungal L-arabinose catabolic pathway,
RT identification of the L-xylulose reductase gene.";
RL Biochemistry 41:6432-6437(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56765 / Rut C-30;
RG DOE Joint Genome Institute;
RA Kuo A., Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION, CATALYTIC ACTIVITY, FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX PubMed=19303876; DOI=10.1016/j.febslet.2009.03.027;
RA Metz B., de Vries R.P., Polak S., Seidl V., Seiboth B.;
RT "The Hypocrea jecorina (syn. Trichoderma reesei) lxr1 gene encodes a D-
RT mannitol dehydrogenase and is not involved in L-arabinose catabolism.";
RL FEBS Lett. 583:1309-1313(2009).
CC -!- FUNCTION: D-mannitol 2-dehydrogenase which is not necessary for D-
CC mannitol catabolism. D-mannitol metabolism occurs via at least two
CC different routes involving mannitol dehydrogenase (MDH) or mannitol 1-
CC phosphate dehydrogenase, and the exact physiological role of mannitol
CC dehydrogenases remains unclear. {ECO:0000269|PubMed:19303876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol + NADP(+) = D-fructose + H(+) + NADPH;
CC Xref=Rhea:RHEA:16765, ChEBI:CHEBI:15378, ChEBI:CHEBI:16899,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.138; Evidence={ECO:0000269|PubMed:19303876};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O93868}.
CC -!- INDUCTION: Exhibits low expression levels on L-arabinose and L-
CC arabitol, as well as on D-mannitol. Transcript levels are shortly up-
CC regulated during the initial stages of germination.
CC {ECO:0000269|PubMed:19303876}.
CC -!- DISRUPTION PHENOTYPE: Does not affect growth on L-arabinose and L-
CC xylulose reductase activity remains unaltered whereas D-mannitol 2-
CC dehydrogenase activity is reduced. Deletion does neither affect the
CC germination process nor the hyphal morphology. Only during later stages
CC mannitol levels are slightly lower. {ECO:0000269|PubMed:19303876}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- CAUTION: Was previously described as the first fungal L-xylulose
CC reductase responsible for NADPH dependent reduction of L-xylulose to
CC xylitol in L-arabinose catabolism (PubMed:12009906). However, lxr1
CC forms a clade with fungal D-mannitol 2-dehydrogenases, is not induced
CC by L-arabinose, and deletion reduces D-mannitol 2-dehydrogenase
CC activity, suggesting that lxr1 is a D-mannitol 2-dehydrogenase and that
CC a true L-xylulose reductase is still awaiting discovery
CC (PubMed:19303876). {ECO:0000269|PubMed:12009906,
CC ECO:0000269|PubMed:19303876}.
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DR EMBL; KI911139; ETS06838.1; -; Genomic_DNA.
DR EMBL; AF375616; AAM20896.1; -; mRNA.
DR AlphaFoldDB; Q8NK50; -.
DR SMR; Q8NK50; -.
DR PRIDE; Q8NK50; -.
DR EnsemblFungi; ETS06838; ETS06838; M419DRAFT_121678.
DR KEGG; trr:M419DRAFT_121678; -.
DR OMA; ITYNSRA; -.
DR BioCyc; MetaCyc:MON-13194; -.
DR BRENDA; 1.1.1.10; 6451.
DR GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0050085; F:mannitol 2-dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0019594; P:mannitol metabolic process; IDA:UniProtKB.
DR GO; GO:0005997; P:xylulose metabolic process; ISS:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; NADP; Oxidoreductase.
FT CHAIN 1..266
FT /note="NADP-dependent mannitol dehydrogenase"
FT /id="PRO_0000054558"
FT ACT_SITE 159
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 178
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 107
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
SQ SEQUENCE 266 AA; 28478 MW; 1CF56334DA86F109 CRC64;
MPQPVPTANR LLDLFSLKGK VVVVTGASGP RGMGIEAARG CAEMGADLAI TYSSRKEGAE
KNAEELTKEY GVKVKVYKVN QSDYNDVERF VNQVVSDFGK IDAFIANAGA TANSGVVDGS
ASDWDHVIQV DLSGTAYCAK AVGAHFKKQG HGSLVITASM SGHVANYPQE QTSYNVAKAG
CIHLARSLAN EWRDFARVNS ISPGYIDTGL SDFIDEKTQE LWRSMIPMGR NGDAKELKGA
YVYLVSDASS YTTGADIVID GGYTTR
