MTLD_PODAN
ID MTLD_PODAN Reviewed; 397 AA.
AC B2AND4; A0A090DAH0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE Short=M1PDH;
DE Short=MPD;
DE Short=MPDH;
DE EC=1.1.1.17;
GN OrderedLocusNames=Pa_6_10260; ORFNames=PODANS_6_10260;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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; CU633872; CAP65533.1; -; Genomic_DNA.
DR EMBL; FO904941; CDP31528.1; -; Genomic_DNA.
DR RefSeq; XP_003437448.1; XM_003437400.1.
DR AlphaFoldDB; B2AND4; -.
DR SMR; B2AND4; -.
DR STRING; 515849.B2AND4; -.
DR EnsemblFungi; CAP65533; CAP65533; PODANS_6_10260.
DR GeneID; 11176499; -.
DR KEGG; pan:PODANS72p234; -.
DR VEuPathDB; FungiDB:PODANS_6_10260; -.
DR eggNOG; ENOG502QVPN; Eukaryota.
DR HOGENOM; CLU_036089_0_1_1; -.
DR OrthoDB; 1133390at2759; -.
DR Proteomes; UP000001197; Chromosome 6.
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; 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 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..397
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000371535"
FT ACT_SITE 220
FT /evidence="ECO:0000250"
FT BINDING 9..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 44155 MW; 1CA27B417CFEA4ED CRC64;
MERNTPKKAV HFGAGNIGRG FVACFLHESG YEVIFAEVND ATVSKLNTHK SYKVIEVGAE
GTTEKTITNY RAINSRSNEA ALVEEIATAD VVTCSVGPNI LKFLAPVIAK GLAARSTDLT
PAAVIACENA IGATDTLAEF IKSPENTNPA LLEDYDKRAT FANSAIDRIV PAQDPDAGLD
VKLEKFYEWV VEKTPFKEWA VPDIKGIKWV DNLQPFIERK LYTVNTGHAT AAYYGYTRRK
STVYDALQDK DIRDEVKNAL KETADLITEK HGIDEEEQKQ YVDKIVRRIS NPHLEDAVER
VGRAPLRKLS RKERFIGPAA ELAENGKDCS ALLDAAEMAF RFQNVEGDDE SFELAKIMEE
KKPEEVVQEV CGLQPSEKLY PQVVDIVKRV QADSNEE
