MTLD_MYCMS
ID MTLD_MYCMS Reviewed; 328 AA.
AC P55800;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE EC=1.1.1.17;
GN Name=mtlD; OrderedLocusNames=MSC_0017;
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1;
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-328.
RC STRAIN=L2;
RX PubMed=9004514; DOI=10.1099/13500872-142-12-3515;
RA Cheng X., Nicolet J., Miserez R., Kuhnert P., Krampe M., Pilloud T.,
RA Abdo E.-M., Griot C., Frey J.;
RT "Characterization of the gene for an immunodominant 72 kDa lipoprotein of
RT Mycoplasma mycoides subsp. mycoides small colony type.";
RL Microbiology 142:3515-3524(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; BX293980; CAE76670.1; -; Genomic_DNA.
DR EMBL; U61140; AAC44573.1; -; Genomic_DNA.
DR RefSeq; NP_975028.1; NC_005364.2.
DR AlphaFoldDB; P55800; -.
DR SMR; P55800; -.
DR STRING; 272632.MSC_0017; -.
DR EnsemblBacteria; CAE76670; CAE76670; MSC_0017.
DR KEGG; mmy:MSC_0017; -.
DR PATRIC; fig|272632.4.peg.17; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_14; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000001016; Chromosome.
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 InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR023027; Mannitol_DH_CS.
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.
DR PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..328
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000170711"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 176
FT /note="S -> R (in Ref. 2; AAC44573)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="F -> L (in Ref. 2; AAC44573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 38565 MW; 9995F74B7577876C CRC64;
MNLIHFGAGN IGCGFIAPIL SSIVDHIYFV DNNIDIVNKI NTQKLIKIHT SDSKKISITN
ISAWLLTDFI NYKKTWNEVS LLTISIGIKN LKHIIYYVNQ LIDYKIKNNQ KLIIMCCENG
IRVSSLFKSY FSNLNNNIYF VDVLVDRIVS NKNILNDYLE CEDYYLWIVD KTQLPSDFKQ
VPNLTYTTSF DIQITKKIYM LNALHCSLAW FVFKNFSFNK YLYVYQALKN DKVVEFVNNY
LNEVILVLNH KYNINLDELN NYKNQIIKRL NSNFIKDDLK RLARNTELKL SKNERILTIL
DYAKDNNLKH DILLLSYQNG LEYLKNNK
