ID A0A0H4PKJ6_9BACI Unreviewed; 387 AA.
AC A0A0H4PKJ6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=BSM4216_3340 {ECO:0000313|EMBL:AKP48522.1};
OS Bacillus smithii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP48522.1, ECO:0000313|Proteomes:UP000036353};
RN [1] {ECO:0000313|EMBL:AKP48522.1, ECO:0000313|Proteomes:UP000036353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP48522.1,
RC ECO:0000313|Proteomes:UP000036353};
RA Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA van Kranenburg R.;
RT "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT 4216T.";
RL Submitted (JUL-2015) 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; CP012024; AKP48522.1; -; Genomic_DNA.
DR RefSeq; WP_048624065.1; NZ_CP012024.1.
DR AlphaFoldDB; A0A0H4PKJ6; -.
DR STRING; 1479.BSM4216_3340; -.
DR KEGG; bsm:BSM4216_3340; -.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000036353; 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,
KW ECO:0000313|EMBL:AKP48522.1}.
FT DOMAIN 2..124
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 150..365
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 387 AA; 43611 MW; B91F79A534FB9652 CRC64;
MLAVHFGAGN IGRGFIGNLL YHSGYEICFV DVNSEIVDLL NEKREYRVGI ADHSQDELVI
KNVRAINSQK NMDQVVEAIA QADLVTAAVG PNILPHIAGA IAEGLRKRIQ TTDKPLNIIA
CENMIGGSTF LKEKVYEKLN EEEKELFNQR FGFPDAAVDR IVPNQSHEDK LKVTVEPFYE
WAVDQTKIVG EKPPVEGITF VDDLNPYIER KLFTVNTGHA VAAYLGYYAG ISTINEAMEK
EEIRTLVEKT LQETGMLLVK KYGFDMKKHQ EYISKIMNRF SNPYISDEVT RVGRSPIRKL
GPNDRLVSPA KQFASVVGER PVYLAKSIAA ALMYDYPQDK EAVEIQESIQ KNGLESTIEH
YTKIDRKSDL AALIVEQYQL LKNKQLI
//
