ID A0A1H1P6Y9_9BACL Unreviewed; 382 AA.
AC A0A1H1P6Y9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05444162_0664 {ECO:0000313|EMBL:SDS06952.1};
OS Paenibacillaceae bacterium GAS479.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae.
OX NCBI_TaxID=1882832 {ECO:0000313|EMBL:SDS06952.1, ECO:0000313|Proteomes:UP000198637};
RN [1] {ECO:0000313|EMBL:SDS06952.1, ECO:0000313|Proteomes:UP000198637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS479 {ECO:0000313|EMBL:SDS06952.1,
RC ECO:0000313|Proteomes:UP000198637};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; LT629764; SDS06952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1P6Y9; -.
DR STRING; 1882832.SAMN05444162_0664; -.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000198637; Chromosome i.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198637}.
FT DOMAIN 1..122
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 151..364
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00196"
SQ SEQUENCE 382 AA; 41384 MW; B8E9E8CA13BF026B CRC64;
MKAVHFGAGN IGRGFIGLLL SQGGYEVIFS DVNERLVEEL KQRGEYTVTL AEEGASGIQV
TGVTAIDGRD PTAVAEAVAS ADLITTAVGV NILKHIAPGI AAGLKLRLQR GGEPLHLIAC
ENAIGASAQL KEQVLALLQP EEAAAVSAMA AFPDSAVDRI VPLQHHEDPL AVTVEPFYEW
VINRSQMLPG AEELPGVHYV DDLIPFIERK LFTVNTGHCS AAYAGYSKGY ATIQESMKDE
DIAAFVQSVL KESGDMLIEA YGFHRAEHEA YILKILDRFR NPYLTDEVVR VGRSPLRKLS
HEDRLVRPAL RALELGLPAQ RLAEAMALAM RFDESSDPEA NQLQESIREL GPVGALAAAS
ELPQEHPLVV AAVSRYNELP KL
//
