MTLD_VIBC3
ID MTLD_VIBC3 Reviewed; 384 AA.
AC A5F155; C3M6Y6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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};
GN OrderedLocusNames=VC0395_0195, VC395_A1069;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000626; ABQ18635.1; -; Genomic_DNA.
DR EMBL; CP001236; ACP11899.1; -; Genomic_DNA.
DR RefSeq; WP_000739122.1; NZ_JAACZH010000003.1.
DR AlphaFoldDB; A5F155; -.
DR SMR; A5F155; -.
DR STRING; 345073.VC395_A1069; -.
DR EnsemblBacteria; ABQ18635; ABQ18635; VC0395_0195.
DR GeneID; 57742397; -.
DR KEGG; vco:VC0395_0195; -.
DR KEGG; vcr:VC395_A1069; -.
DR PATRIC; fig|345073.21.peg.3792; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_6; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000000249; Chromosome 1.
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.
FT CHAIN 1..384
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_1000071712"
FT BINDING 5..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 384 AA; 42340 MW; 60D4F90913EF186D CRC64;
MKKNAVHFGA GNIGRGFIGK LLADADIAVT FADVNEPLVD QLSHQQEYKV KVVGSECKME
TVSHVTAVNS ASEALIERII KTDLVTTAVG PTVLDIIAKT IAKGLSARFA AGNTQPLNII
ACENMVRGTT HLKQQVYQFL TTEEQQQADA LVGFVDSAVD RIVPPLQAAN DDPLEVTVES
FSEWIVDEQQ FKGEIPQIEG MEKTDNLMAF VERKLFTLNT GHCVTAYLGC LKGHRTIREA
IEDPCIHAQV KQAMQESGEV LIRRYGFDRA LHSAYIEKIL SRFANPYLVD EVDRVGRQPL
RKLSANDRLI KPLLGTIEYG LPNGMLLKGI AAALKYRNSS DPQAVELQQS IEKEGVRSTL
ARYTGLAAES VEAQQIEALY QQMD
