MTLD_STAAW
ID MTLD_STAAW Reviewed; 368 AA.
AC P63956; Q99SA1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=MW2085;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB95950.1; -; Genomic_DNA.
DR RefSeq; WP_000648723.1; NC_003923.1.
DR AlphaFoldDB; P63956; -.
DR SMR; P63956; -.
DR EnsemblBacteria; BAB95950; BAB95950; BAB95950.
DR KEGG; sam:MW2085; -.
DR HOGENOM; CLU_036089_2_0_9; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000000418; 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.
FT CHAIN 1..368
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000170724"
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; 40936 MW; 3A6FC0F3984E46ED CRC64;
MKAVHFGAGN IGRGFIGYIL ADNNVKVTFA DVNEEIINAL AHDHQYDVIL ADESKTTTRV
NNVDAINSMQ PSEALKQAIL EADIITTAVG VNILPIIAKS FAPFLKEKTN HVNIVACENA
IMATDTLKKA VLDITGPLGN NIHFANSAVD RIVPLQKNEN ILDVMVEPFY EWVVEKDAWY
GPELNHIKYV DDLTPYIERK LLTVNTGHAY LAYAGKFAGK ATVLDAVKDS SIEAGLRRVL
AETSQYITNE FDFTEAEQAG YVEKIIDRFN NSYLSDEVTR VGRGTLRKIG PKDRIIKPLT
YLYNKDLERT GLLNTAALLL KYDDTADQET VEKNNYIKEH GLKAFLSEYA KVDDGLADEI
IEAYNSLS