MTLD_STAA8
ID MTLD_STAA8 Reviewed; 368 AA.
AC Q2FW96;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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};
GN OrderedLocusNames=SAOUHSC_02403;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD31432.1; -; Genomic_DNA.
DR RefSeq; WP_000648719.1; NZ_LS483365.1.
DR RefSeq; YP_500879.1; NC_007795.1.
DR PDB; 5JNM; X-ray; 1.70 A; A=1-368.
DR PDBsum; 5JNM; -.
DR AlphaFoldDB; Q2FW96; -.
DR SMR; Q2FW96; -.
DR STRING; 1280.SAXN108_2403; -.
DR EnsemblBacteria; ABD31432; ABD31432; SAOUHSC_02403.
DR GeneID; 3919618; -.
DR KEGG; sao:SAOUHSC_02403; -.
DR PATRIC; fig|93061.5.peg.2175; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_9; -.
DR OMA; GKKAVHF; -.
DR PRO; PR:Q2FW96; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0019592; P:mannitol catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..368
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_1000011814"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 368 AA; 40937 MW; 3A6FCAF33FF8EB5B CRC64;
MKAVHFGAGN IGRGFIGYIL ADNNVKVTFA DVNEEIINAL AHDHQYDVIL ADESKTTTRV
NNVDAINSMQ PSEALKQAIL EADIITTAVG VNILPIIAKS FAPFLKEKTN HVNIVACENA
IMATDTLKKA VLDITGPLGN NIHFANSAVD RIVPLQKNEN ILDVMVEPFY EWVVEKDAWY
GPELNHIKYV DDLTPYIERK LLTVNTGHAY LAYAGKFAGK ATVLDAVEDS SIEAGLRRVL
AETSQYITNE FDFTEAEQAG YVEKIIDRFN NSYLSDEVTR VGRGTLRKIG PKDRIIKPLT
YLYNKDLERT GLLNTAALLL KYDDTADQET VEKNNYIKEH GLKAFLSEYA KVDDGLADEI
IEAYNSLS
