ID MTLD_NEOFI Reviewed; 388 AA.
AC A1DGY9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 85.
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=mpdA; ORFNames=NFIA_086010;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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. {ECO:0000250}.
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}.
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DR EMBL; DS027696; EAW18646.1; -; Genomic_DNA.
DR RefSeq; XP_001260543.1; XM_001260542.1.
DR AlphaFoldDB; A1DGY9; -.
DR SMR; A1DGY9; -.
DR STRING; 331117.A1DGY9; -.
DR EnsemblFungi; EAW18646; EAW18646; NFIA_086010.
DR GeneID; 4587101; -.
DR KEGG; nfi:NFIA_086010; -.
DR VEuPathDB; FungiDB:NFIA_086010; -.
DR eggNOG; ENOG502QVPN; Eukaryota.
DR HOGENOM; CLU_036089_0_1_1; -.
DR OMA; APFIERK; -.
DR OrthoDB; 1700931at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 PANTHER; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..388
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000371529"
FT ACT_SITE 213
FT /evidence="ECO:0000250"
FT BINDING 5..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 388 AA; 42891 MW; AECBA22D7475D657 CRC64;
MGKKAIQFGG GNIGRGFVAE FLHEAGYEVV FIDVVDKIID ALKSTPSYEV SEVSEEGEKT
KTITNYRAIN SKTNEEDVVK EIGTADVVTC AVGPNVLKFI APVIAKGIDA RTASKPVAVI
ACENAIGATD TLRGFIEQHT DKDRLSSMSE RARFANSAID RIVPNQPPNA GLNVRIEKFY
EWTVEQTPFG EFGHPDIPAI HWVDDLKPYI ERKLFTVNTG HATTAYYGHV RGKKMIADAL
ADAEIRKIVH NVLEQTAMLI TTKHEITEQE QNEYVDTIVK RMSNPFLEDN VERVGRAPLR
KLSRNERFIG PASQLAEKGL PFDALLGSIE MALRFQNVPG DEESAELAKI LKEMSADEAT
GKLTGLEKSH PLYKPVQNVV AKVQKDSK
//
