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MTLD_MYCPN
ID   MTLD_MYCPN              Reviewed;         364 AA.
AC   P78008;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            EC=1.1.1.17;
GN   Name=mtlD; OrderedLocusNames=MPN_652; ORFNames=MP190;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U00089; AAB95838.1; -; Genomic_DNA.
DR   PIR; S73516; S73516.
DR   RefSeq; NP_110341.1; NC_000912.1.
DR   RefSeq; WP_010875009.1; NC_000912.1.
DR   AlphaFoldDB; P78008; -.
DR   SMR; P78008; -.
DR   IntAct; P78008; 1.
DR   STRING; 272634.MPN_652; -.
DR   EnsemblBacteria; AAB95838; AAB95838; MPN_652.
DR   KEGG; mpn:MPN_652; -.
DR   PATRIC; fig|272634.6.peg.716; -.
DR   HOGENOM; CLU_036089_2_0_14; -.
DR   OMA; GKKAVHF; -.
DR   BioCyc; MetaCyc:MON-622; -.
DR   BioCyc; MPNE272634:G1GJ3-1039-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-UniRule.
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; 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   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..364
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000170712"
FT   BINDING         6..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  42271 MW;  199394BBF11E31B6 CRC64;
     MKRINVLHFG AGNIGRGVIL PIYQQNDFSI DLVELNQNTV NELQKQKQYQ VHYLDCDQSQ
     LVNDFNTWNL KDEAKIIELM ERADVISTSI GAKNLASLKT LFDKAKFHKR AIVLCFENGF
     RISSNFKNIL QLNNTQVNFV DVVIDTIAPN FEKKANFLDI YCEKYSEIYA ETFPLEIKGV
     NQKNSLDRFI IKKLLLVNAL HSVIGLLGFQ QKLKYVHETL QVKSNLTFVE KLAQQIIDAL
     CAEYPEFNKN NLLSYGKNNL VRFANPKIQD LNTRLIREPL RKLNQNERFY AIYKLFKKNK
     IALNNILQVY LMVLKTNITD DTESQQIAKL INEKAWTELA KLSSLEESEW NLIKQELSRE
     ITKK
 
 
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