MTLD_VIBPA
ID MTLD_VIBPA Reviewed; 382 AA.
AC Q87SQ3;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
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}; OrderedLocusNames=VP0369;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC58632.1; -; Genomic_DNA.
DR RefSeq; NP_796748.1; NC_004603.1.
DR RefSeq; WP_005480503.1; NC_004603.1.
DR AlphaFoldDB; Q87SQ3; -.
DR SMR; Q87SQ3; -.
DR STRING; 223926.28805352; -.
DR DNASU; 1187836; -.
DR EnsemblBacteria; BAC58632; BAC58632; BAC58632.
DR GeneID; 1187836; -.
DR KEGG; vpa:VP0369; -.
DR PATRIC; fig|223926.6.peg.355; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_6; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000002493; 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; Reference proteome.
FT CHAIN 1..382
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000170730"
FT BINDING 4..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 382 AA; 41978 MW; 9F5C141DF6769F0F CRC64;
MKNAVHFGAG NIGRGFIGKL LADAEVEVTF ADVDVPLVDQ LSHKQEYKVK VVGTECKIDT
VTHVTAVNSA SEDVIDRIVK TDLVTTAVGP NVLDIIAKTI AKGIAKRFEA GNDAPLNIIA
CENMVRGTTH LKGEVYKHLD KSLHAKADEL VGFVDSAVDR IVPPAEAAND DPLEVTVESF
SEWIVDEQQF KGDIPNIAGM EKTNNLMAFV ERKLFTLNTG HCITAYLGCL KGHRTIREAI
EDPNIHAEVK QAMQESGEVL IRRYGFDHDM HNAYIEKILG RFANPYLVDE VDRVGRQPIR
KLGANDRLVK PLLGTIEYGT ENQTLLKGIA AALKYTNDTD PQAVELQTSL KEVGVTKTLA
KYTGLAEDSD EVAQIETLYN QL
