ID A0A1W5ZQP5_9BACI Unreviewed; 391 AA.
AC A0A1W5ZQP5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000256|ARBA:ARBA00016219, ECO:0000256|HAMAP-Rule:MF_00196};
DE EC=1.1.1.17 {ECO:0000256|ARBA:ARBA00012939, ECO:0000256|HAMAP-Rule:MF_00196};
GN Name=mtlD {ECO:0000256|HAMAP-Rule:MF_00196};
GN ORFNames=HM131_01665 {ECO:0000313|EMBL:ARI75609.1};
OS Halobacillus mangrovi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=402384 {ECO:0000313|EMBL:ARI75609.1, ECO:0000313|Proteomes:UP000192527};
RN [1] {ECO:0000313|EMBL:ARI75609.1, ECO:0000313|Proteomes:UP000192527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTB 131 {ECO:0000313|EMBL:ARI75609.1,
RC ECO:0000313|Proteomes:UP000192527};
RA Lee S.-J., Park M.-K., Kim J.-Y., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F.,
RA Lee D.-W.;
RT "The whole genome sequencing and assembly of Halobacillus mangrovi
RT strain.";
RL Submitted (APR-2017) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000292, ECO:0000256|HAMAP-
CC Rule:MF_00196};
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_00196}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00196}.
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DR EMBL; CP020772; ARI75609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5ZQP5; -.
DR STRING; 402384.HM131_01665; -.
DR KEGG; hmn:HM131_01665; -.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000192527; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00196};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00196}.
FT DOMAIN 1..123
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 149..366
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 391 AA; 44077 MW; 02493758008D2A32 CRC64;
MKALHFGAGN IGKGLIGYLL NKSGFDLCFV DVNEDSVNRM NRSNNYSLEL LDENQTVEVI
SPVCALHSSA QEKVVEAIVE ADLITTSVGA DNLSKVAPVI SKGLLKRIQS DKGNVDVIAN
ENMINASSKL KDEIRRNVSE NEMDTIESTV GFPNSAIDRL SLSEKRSEGE VTLVEPYYEW
MIEKQGMLNS DLPSIENATY VDSLKPYIER KLYIVNLGHA ATAYTAFLKG YSTIQSALEN
PEIEKFLRET LNESARYFTH HYDFESEEMS EFIEKTIARF KNANISDDIL RVGRSPIRKL
GFDERLTKPT RVLFELGLPV ERLTAAVATA FFFHNPDDKE SVTIQSYIRE QGIEQAIAHF
TEIEDATLQS KIKDHYSRLK ENDSLLTINE R
//
