MTLD_ASPTN
ID MTLD_ASPTN Reviewed; 388 AA.
AC Q0CXS6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=ATEG_01508;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476595; EAU38265.1; -; Genomic_DNA.
DR RefSeq; XP_001208873.1; XM_001208873.1.
DR AlphaFoldDB; Q0CXS6; -.
DR SMR; Q0CXS6; -.
DR STRING; 341663.Q0CXS6; -.
DR EnsemblFungi; EAU38265; EAU38265; ATEG_01508.
DR GeneID; 4315529; -.
DR VEuPathDB; FungiDB:ATEG_01508; -.
DR eggNOG; ENOG502QVPN; Eukaryota.
DR HOGENOM; CLU_036089_0_1_1; -.
DR OMA; GKKAVHF; -.
DR OrthoDB; 1133390at2759; -.
DR Proteomes; UP000007963; 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; 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..388
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000371524"
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; 42864 MW; F9A1A47CE4A697AC CRC64;
MGKKAIQFGG GNIGRGFVAE FLHEAGYEVV FVDVMDAVVS ALQTTPSYNV TEVSKDGENT
KTISNYRAIN SKTNESDAVK EIATADVVTC AVGPNILKFI APLIAKGIDA RTESKPVAVI
ACENAIGATD TLHGFIKEHT PKDRLDTLYD RARFANSAID RIVPNQPPNS GLNVRIEKFY
EWAVEQTPFG SFGHPDIPAI HWVDNLEPYI ERKLFTVNTG HATTAYYGHL RGKKMIADAL
ADDEIRSMVH KVLDETASLI VSKHGIPEDE QKEYVDTIIG RMSNPYLEDN IERVGRAPLR
KLSRKERFIG PASQLAERGQ KFDALVDAIE MALRFQNVPG DQESADLAQI LKQKSSEDAT
SELTGLEKDH PLYSPVLERV AKVQQDTK