MTLD_PHANO
ID MTLD_PHANO Reviewed; 390 AA.
AC Q0U6E8; B6DQL1; Q5DQ93;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE Short=M1PDH;
DE Short=MPD;
DE Short=MPDH;
DE EC=1.1.1.17;
GN Name=mpd1; ORFNames=SNOG_12666;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=15720079; DOI=10.1094/mpmi-18-0110;
RA Solomon P.S., Tan K.-C., Oliver R.P.;
RT "Mannitol 1-phosphate metabolism is required for sporulation in planta of
RT the wheat pathogen Stagonospora nodorum.";
RL Mol. Plant Microbe Interact. 18:110-115(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-389.
RC STRAIN=S-81-B13B, and Sn37-1;
RA Malkus A., Chiu E.Y., Ueng P.P.;
RT "Genetic mapping of Phaeosphaeria nodorum.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=16859492; DOI=10.1042/bj20060891;
RA Solomon P.S., Waters O.D.C., Joergens C.I., Lowe R.G.T., Rechberger J.,
RA Trengove R.D., Oliver R.P.;
RT "Mannitol is required for asexual sporulation in the wheat pathogen
RT Stagonospora nodorum (glume blotch).";
RL Biochem. J. 399:231-239(2006).
CC -!- FUNCTION: Catalyzes the NAD(H)-dependent interconversion of D-fructose
CC 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic
CC pathway. Required for the process of sporulation on senescing leaf
CC material. {ECO:0000269|PubMed:15720079, ECO:0000269|PubMed:16859492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61381; EC=1.1.1.17;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {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; AY547308; AAT11122.1; -; mRNA.
DR EMBL; CH445347; EAT79964.1; -; Genomic_DNA.
DR EMBL; FJ151548; ACI04508.1; -; Genomic_DNA.
DR EMBL; FJ151549; ACI04509.1; -; Genomic_DNA.
DR RefSeq; XP_001802887.1; XM_001802835.1.
DR AlphaFoldDB; Q0U6E8; -.
DR SMR; Q0U6E8; -.
DR STRING; 13684.SNOT_12666; -.
DR EnsemblFungi; SNOT_12666; SNOT_12666; SNOG_12666.
DR GeneID; 5979798; -.
DR KEGG; pno:SNOG_12666; -.
DR eggNOG; ENOG502QVPN; Eukaryota.
DR HOGENOM; CLU_036089_0_1_1; -.
DR InParanoid; Q0U6E8; -.
DR OMA; GKKAVHF; -.
DR OrthoDB; 1133390at2759; -.
DR BRENDA; 1.1.1.17; 7864.
DR PHI-base; PHI:2249; -.
DR PHI-base; PHI:2270; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0019592; P:mannitol catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_00196; Mannitol_dehydrog; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR023028; Mannitol_1_phos_5_DH.
DR InterPro; IPR000669; Mannitol_DH.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..390
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000371534"
FT ACT_SITE 216
FT /evidence="ECO:0000250"
FT BINDING 7..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 101
FT /note="F -> L (in Ref. 1; AAT11122)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="E -> K (in Ref. 1; AAT11122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43475 MW; 272D3357DEDE8278 CRC64;
MPYDKKAVHF GGGNIGRGFV AEFLHNSGYE VVFVDVMDSI IEALQKQSSY TVTEIGDDGE
REFTIDHYRA LNSKHEMDKV VQEIASADVV TCAVGPNILK FVAEPVAKAI DARTLDYPIA
VIACENAINA TTTWRGFIEG KLSEDSKSNL DKKARFANSA IDRIVPVQDK DAGLNVKIEK
FYEWCVEQKP FENGGKKPDV KGIHYVDDLE PYIERKLFTV NTSHATAAYY GHQAKKQYIH
EVLQDKKLHD IVRDAVKETA HLIVSKHGVS VQEQNDYVDS IIKRISNPVL KDNVERVGRA
PLRKLSRKER FVGPAAQLAE RGEKVDALLG AIEQAYLFQN VEGDEESAEL AKILKENSAE
EVVTKVNGLD KSHPLFEKIL PIVKKVQGGS
