ID V7I8K5_9CLOT Unreviewed; 381 AA.
AC V7I8K5;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=T472_0205790 {ECO:0000313|EMBL:ETA81579.1};
OS Youngiibacter fragilis 232.1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Youngiibacter.
OX NCBI_TaxID=994573 {ECO:0000313|EMBL:ETA81579.1, ECO:0000313|Proteomes:UP000017747};
RN [1] {ECO:0000313|EMBL:ETA81579.1, ECO:0000313|Proteomes:UP000017747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232.1 {ECO:0000313|EMBL:ETA81579.1,
RC ECO:0000313|Proteomes:UP000017747};
RX PubMed=24459265;
RA Wawrik C.B., Callaghan A.V., Stamps B.W., Wawrik B.;
RT "Genome Sequence of Youngiibacter fragilis, the Type Strain of the Genus
RT Youngiibacter.";
RL Genome Announc. 2:e01183-13(2014).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETA81579.1}.
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DR EMBL; AXUN02000090; ETA81579.1; -; Genomic_DNA.
DR RefSeq; WP_023383401.1; NZ_AXUN02000090.1.
DR AlphaFoldDB; V7I8K5; -.
DR STRING; 994573.T472_0205790; -.
DR PATRIC; fig|994573.3.peg.1085; -.
DR eggNOG; COG0246; Bacteria.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000017747; Unassembled WGS sequence.
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; IPR023027; Mannitol_DH_CS.
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.
DR PROSITE; PS00974; MANNITOL_DHGENASE; 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:UP000017747}.
FT DOMAIN 2..125
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 153..372
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
FT BINDING 4..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00196"
SQ SEQUENCE 381 AA; 42077 MW; D900B637341BA542 CRC64;
MMKALHFGAG NIGRGFIGLI LRQNGYELTF ADISDTLIDE IKAKKEYDVI IADPTGRVIH
VDGVDAVHNV KEADRLKSLV EEADLITTAV GPSIVPIVAK TIAEGIKERL SRQDVKPLNI
IACENAIGAT DTLKEALYGY LSELETGIAE VAIGFPNSAV DRIVPAQNNA NLLDVKVEPF
FEWVIEEKKL RGAHPKIEGV HYVDDLIPYI ERKLFTVNTG HAATAYLGAQ KGFTTVFDAI
GDPEIEASVR AVLDETSQYI TGYYGFDKEE HAKYVDTIIG RFKNPDISDD LERVGRSPLR
KISKYDRFVN PALRLLDMGI EPKSIAKAIA AALRFRAESD RESLELNNFV KENGVREALI
KYSSLAPDSK LIDLVEEAYN A
//
