MTLD_NEUCR
ID MTLD_NEUCR Reviewed; 398 AA.
AC Q7SA44;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE Short=M1PDH;
DE Short=MPD;
DE Short=MPDH;
DE EC=1.1.1.17;
GN ORFNames=NCU07318;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002239; EAA33240.1; -; Genomic_DNA.
DR RefSeq; XP_962476.1; XM_957383.3.
DR AlphaFoldDB; Q7SA44; -.
DR SMR; Q7SA44; -.
DR STRING; 5141.EFNCRP00000007185; -.
DR EnsemblFungi; EAA33240; EAA33240; NCU07318.
DR GeneID; 3878624; -.
DR KEGG; ncr:NCU07318; -.
DR VEuPathDB; FungiDB:NCU07318; -.
DR HOGENOM; CLU_036089_0_1_1; -.
DR InParanoid; Q7SA44; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..398
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000371530"
FT ACT_SITE 221
FT /evidence="ECO:0000250"
FT BINDING 10..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 44372 MW; 506D426F92E1A396 CRC64;
MAANNYTKKA VHFGAGNIGR GFVACFLHNS GYEVIFADVN ADLINALNAS PSYKVIEVGS
EGTEESTITN YRAINSRTNE EELIQEIATA EVVTCSVGPN ILKFIAPVIA KGIDRRSEDL
PPVAVIACEN AIGATDTLAE YIKDPKNTPS HRLENYEKRA RFANSAIDRI VPAQDADAGL
DVKLEKFYEW VVDRTPFKDM SPPDIKGINW VDNLLPYIER KLYTVNTGHA TAAYHGYIRR
KSTVYDALQD KDIQEEVKKA LENTSHLITQ KHGIDEQAQH EYVEKIVRRI SNPHLEDAVE
RVGRAPLRKL SRKERFIGPA AELAEHGKDC SALLDAAEMA FRFQNVEGDE ESAELAKIMA
SNKPEDVVKQ VCGLNEQEKL FPKVVEVVQR VQADLHDD