ID MTLD_STAAS Reviewed; 368 AA. AC Q6G7F3; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 16-JUN-2009, entry version 26. DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase; DE EC=1.1.1.17; GN Name=mtlD; OrderedLocusNames=SAS2060; OS Staphylococcus aureus (strain MSSA476). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). CC -!- CATALYTIC ACTIVITY: D-mannitol 1-phosphate + NAD(+) = D-fructose CC 6-phosphate + NADH. CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571857; CAG43869.1; -; Genomic_DNA. DR RefSeq; YP_044171.1; -. DR GeneID; 2862820; -. DR GenomeReviews; BX571857_GR; SAS2060. DR KEGG; sas:SAS2060; -. DR HOGENOM; Q6G7F3; -. DR OMA; Q6G7F3; VDRIVPN. DR BioCyc; SAUR282459:SAS2060-MON; -. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00196; -; 1. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR013118; Mannitol_DH_C. DR InterPro; IPR000669; Mannitol_DH_core. DR InterPro; IPR013131; Mannitol_DH_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR Pfam; PF01232; Mannitol_dh; 1. DR Pfam; PF08125; Mannitol_dh_C; 1. DR PRINTS; PR00084; MTLDHDRGNASE. DR PROSITE; PS00974; MANNITOL_DHGENASE; 1. PE 3: Inferred from homology; KW Complete proteome; NAD; Oxidoreductase. FT CHAIN 1 368 Mannitol-1-phosphate 5-dehydrogenase. FT /FTId=PRO_0000170723. FT NP_BIND 3 14 NAD (By similarity). 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 //