MTLD_GEOKA
ID MTLD_GEOKA Reviewed; 387 AA.
AC Q5KYK6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, 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=GK1945;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD76230.1; -; Genomic_DNA.
DR RefSeq; WP_011231431.1; NC_006510.1.
DR AlphaFoldDB; Q5KYK6; -.
DR SMR; Q5KYK6; -.
DR STRING; 235909.GK1945; -.
DR EnsemblBacteria; BAD76230; BAD76230; GK1945.
DR KEGG; gka:GK1945; -.
DR PATRIC; fig|235909.7.peg.2086; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_9; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000001172; 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..387
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_1000011799"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 387 AA; 42363 MW; 513DC6F6976DE6C0 CRC64;
MRAVHFGAGN IGRGFIGSLL AASGYDVVFV DVNEQIVRLL KERGEYRVIV AGEQREEQWV
RGVSALNSQT EREKVIEVIA DADLVTTAVG PPILPAIAPV VAAGLQRRFA IQQKPLHVIA
CENMIAGTEA LKQHVLAHLS EAEQQLASEH VGFLNCAVDR IVPNQTNDDP LAVTVEPFFE
WAIEARNVIG TVPPIQGAHF VADLGPYIER KLFTVNTGHA LAAYLGYLRN YKTVQEAMND
EGIRLNVEQA LSESGAVLVK KHGWSEKEHH AYIDTTIGRF MNPSLSDDIL RVARSPIRKL
GPNDRLVAPA VQYCALFGKV PHGLAKGIAA LLRFDDSRDA EAAALQQTIA QHGIEGALRQ
YAGLESAHPL VAAVREEYDQ MDENKRL