ID MTLD_STRR6 Reviewed; 378 AA. AC Q8DR31; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 31. DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase; DE EC=1.1.1.17; GN Name=mtlD; OrderedLocusNames=spr0359; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21429245; PubMed=11544234; RX DOI=10.1128/JB.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., RA LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., RA McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., RA Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., RA Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., RA Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., RA Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). 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; AE007317; AAK99163.1; -; Genomic_DNA. DR PIR; G97916; G97916. DR RefSeq; NP_357953.1; -. DR GeneID; 933124; -. DR GenomeReviews; AE007317_GR; spr0359. DR KEGG; spr:spr0359; -. DR HOGENOM; Q8DR31; -. DR OMA; Q8DR31; VDRIVPN. DR BioCyc; SPNE171101:SPR0359-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 1 378 Mannitol-1-phosphate 5-dehydrogenase. FT /FTId=PRO_0000170727. FT NP_BIND 4 15 NAD (By similarity). SQ SEQUENCE 378 AA; 42991 MW; 934C2686C51BF5A6 CRC64; MKHSVHFGAG NIGRGFIGEI LFKNGFHIDF VDVNNQIIHA LNEKGKYEIE IAQKGQSRIE VTNVAGINSK EHPEQVIEAI QKTDIITTAI GPNILPFIAE LLAKGIEARR VAGNTQVLDV MACENMIGGS QFLYQEVKKY LSPEGLTFAD NYIGFPNAAV DRIVPAQSHE DSLFVVVEPF NEWVVETKRL KNPDLRLKDV HYEEDLEPFI ERKLFSVNSG HATSAYIGAH YGAKTILEAL QNPNIKSRIE SVLAEIRSLL IAKWNFDKKE LENYHKVIIE RFENPFIVDE VSRVARTPIR KLGYNERFIR PIRELKELSL SYKNLLKTVG YAFDYRDVND EESIRLGELL AKQLVKDVVI QVTGLDDQEL IEQIVEYI //