MTLD_THEP3
ID MTLD_THEP3 Reviewed; 388 AA.
AC B0KCW3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00196};
DE EC=1.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00196};
GN Name=mtlD {ECO:0000255|HAMAP-Rule:MF_00196}; OrderedLocusNames=Teth39_1939;
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00196};
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00196}.
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DR EMBL; CP000924; ABY95570.1; -; Genomic_DNA.
DR RefSeq; WP_012269671.1; NC_010321.1.
DR AlphaFoldDB; B0KCW3; -.
DR SMR; B0KCW3; -.
DR STRING; 340099.Teth39_1939; -.
DR EnsemblBacteria; ABY95570; ABY95570; Teth39_1939.
DR KEGG; tpd:Teth39_1939; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_9; -.
DR OMA; GMNLADN; -.
DR Proteomes; UP000002156; 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; IPR000669; Mannitol_DH.
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 PRINTS; PR00084; MTLDHDRGNASE.
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..388
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_1000099207"
FT BINDING 4..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 388 AA; 44487 MW; 6D50269AA36E401C CRC64;
MLKAVHFGAG NIGRGFIGYL LYKSGYEITF VDISKELVES INNYKRYNVI ILKDNVEKEE
VKNIKAIHIE DEENLSKAIV DADIITTSVG ANNLKSIGEK LRNYLKIRKA NIDKPLNIMA
CENALFATNI LKNSILEKGD KDFIEYVNQK IGFPNTAVDR IVPNVDIKKE LPIDVAVEDF
YEWDIEKKAI IGDLNIKGAE LVDDLEPYIE RKLFLLNGAH ATTAYLGYLK GYKYIHEAIQ
DDFIRNIVSK MQEEASIALS KKHNIKIDNL REYSNKVIKR FKNSYLKDEV VRVGREPTRK
LSGNDRLMMP AKLCYEIGIT PKFILYGIAA GFLFDYKEDP QACKIQDDIK NFGLEKTISK
ITGLEENSDL LHEIVKKYKE LKETFRKR
