MTLD_KLEPN
ID MTLD_KLEPN Reviewed; 382 AA.
AC Q9XBM6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE EC=1.1.1.17;
GN Name=mtlD;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1033-5P14 / KAY2026;
RX PubMed=11164312; DOI=10.1111/j.1574-6968.2001.tb09473.x;
RA Otte S., Lengeler J.W.;
RT "The mtl genes and the mannitol-1-phosphate dehydrogenase from Klebsiella
RT pneumoniae KAY2026.";
RL FEMS Microbiol. Lett. 194:221-227(2001).
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;
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF166095; AAD45386.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9XBM6; -.
DR SMR; Q9XBM6; -.
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..382
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000170707"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 382 AA; 41130 MW; D9927E6C068C5344 CRC64;
MKALHFGAGN IGRGFIGKLL ADAGIELTFA DVNQTVLDAL NARHSYQVHV VGENEQVDTV
SGVNAVSSIG DEVVDLIAEV DVVTTAVGPV ALERIAPAIA KGLAQRKAQG TERPLNIIAC
ENMVRGTTQL KGHVFNALAE EDKAWVEAHI GFVDSAVDRI VPPSASATHD PLEVTVETFS
EWIVDKTQFK GALPTIPGME LTDNLMAFVE RKLFTLNTGH AITAYLGKLA GHQTIRDAIL
DKKIRAVVQG AMEESGAVLI KRYAFDPQKH AAYIQKILGR FENPYLKDDV ERVGRQPLRK
LSAGDRLIKP LLGTLEYGLP HRNLVKGIAA AMHFRSEDDP QAQELAALIA DKGPQAALAQ
ISGLDAASDV VAEAVNDYNA EK