MTDH_UROFA
ID MTDH_UROFA Reviewed; 256 AA.
AC O00058;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Probable NADP-dependent mannitol dehydrogenase;
DE Short=MtDH;
DE EC=1.1.1.138;
DE AltName: Full=Mannitol 2-dehydrogenase [NADP(+)];
DE AltName: Full=Planta-induced rust protein 8;
GN Name=PIG8;
OS Uromyces fabae (Rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Uromyces.
OX NCBI_TaxID=55588;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=I2; TISSUE=Haustorium;
RX PubMed=9150592; DOI=10.1094/mpmi.1997.10.4.427;
RA Hahn M., Mendgen K.;
RT "Characterization of in planta-induced rust genes isolated from a
RT haustorium-specific cDNA library.";
RL Mol. Plant Microbe Interact. 10:427-437(1997).
CC -!- FUNCTION: May be involved in hexitol or pentitol metabolism.
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;
CC -!- DEVELOPMENTAL STAGE: Haustoria and rust-infected leaves.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; U81790; AAB39878.1; -; mRNA.
DR AlphaFoldDB; O00058; -.
DR SMR; O00058; -.
DR PRIDE; O00058; -.
DR GO; GO:0050085; F:mannitol 2-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW NADP; Oxidoreductase.
FT CHAIN 1..256
FT /note="Probable NADP-dependent mannitol dehydrogenase"
FT /id="PRO_0000054729"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT ACT_SITE 167
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 18..21
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 67..68
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 94
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 196
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
SQ SEQUENCE 256 AA; 27842 MW; 218677F0010364D5 CRC64;
MTFTIDLKDQ CIIVTGGNRG IGLAMSQACA DAGAAVGIIY NSAKDAEDRA SEISKKYGVK
CKAYQCDVGQ QHKVKEVFKK INEELGPVTG LIANAGVSVV KEALQYNKDD FNKIFDVNVF
GVFNCAQAMA QIWTDTGFQR GSVVIISSMS SQICNRPLTQ CFYNSSKAAV SNLGKCLAAE
WAEKSIRVNM LSPGYVKTDQ TSHMDQKLRD FQADGVPLKR FAEPEEMAGQ AILLLSPKAS
YMTGGEYFVD GGNLVW
