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