MTLD_KLEP7
ID MTLD_KLEP7 Reviewed; 382 AA.
AC A6TFJ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=KPN78578_39040; ORFNames=KPN_03943;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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; CP000647; ABR79328.1; -; Genomic_DNA.
DR RefSeq; WP_015959133.1; NC_009648.1.
DR AlphaFoldDB; A6TFJ4; -.
DR SMR; A6TFJ4; -.
DR STRING; 272620.KPN_03943; -.
DR jPOST; A6TFJ4; -.
DR DNASU; 5340588; -.
DR EnsemblBacteria; ABR79328; ABR79328; KPN_03943.
DR KEGG; kpn:KPN_03943; -.
DR HOGENOM; CLU_036089_2_0_6; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000000265; 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..382
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_1000011801"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 382 AA; 41195 MW; 5AE6C41420F2040A CRC64;
MKALHFGAGN IGRGFIGKLL ADAGIELTFA DVNQTVLDAL NARHSYQVHV VGENEQVDTV
SGVNAVSSIG DEVVDLIAEV DLVTTAVGPV VLERIAPAIA KGLAQRKAQG TERPLNIIAC
ENMVRGTTQL KGHVFNALAE EHKAWVEAHI GFVDSAVDRI VPPSASATHD PLEVTVETFS
EWIVDKTQFK GALPTIPGME LTDNLMAFVE RKLFTLNTGH AITAYLGKLA GHQTIRDAIL
DEKIRAVVQG AMEESGAVLI KRYAFDPQKH AAYIQKILGR FENPYLKDDV ERVGRQPLRK
LSAGDRLIKP LLGTLEYGLP HRNLVKGIAA AMHFRSEDDP QAQELAALIA DKGPQAALAQ
ISGLDAASDV VAEAVNDYNA EK