[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=3135464 [NCBI, ExPASy, EBI, Israel, Japan] Davis T., Yamada M., Elgort M., Saier M.H. Jr.; "Nucleotide sequence of the mannitol (mtl) operon in Escherichia coli."; Mol. Microbiol. 2:405-412(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION. STRAIN=K12; PubMed=1964486 [NCBI, ExPASy, EBI, Israel, Japan] Jaiang W., Wu L.F., Tomich J., Saier M.H. Jr., Nichaus W.G.; "Corrected sequence of the mannitol (mtl) operon in Escherichia coli."; Mol. Microbiol. 4:2003-2006(1990).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/22.13.2576; PubMed=8041620 [NCBI, ExPASy, EBI, Israel, Japan] Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."; Nucleic Acids Res. 22:2576-2586(1994).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 369-382. STRAIN=K12; PubMed=8300537 [NCBI, ExPASy, EBI, Israel, Japan] Figge R.M., Ramseier T.M., Saier M.H. Jr.; "The mannitol repressor (MtlR) of Escherichia coli."; J. Bacteriol. 176:840-847(1994).
[7]	PROTEIN SEQUENCE OF 1-25. PubMed=6384188 [NCBI, ExPASy, EBI, Israel, Japan] Novotny M.J., Reizer J., Esch F., Saier M.H. Jr.; "Purification and properties of D-mannitol-1-phosphate dehydrogenase and D-glucitol-6-phosphate dehydrogenase from Escherichia coli."; J. Bacteriol. 159:986-990(1984).
[8]	PROTEIN SEQUENCE OF 1-15. PubMed=8899705 [NCBI, ExPASy, EBI, Israel, Japan] Gonzalez-Gil G., Bringmann P., Kahmann R.; "FIS is a regulator of metabolism in Escherichia coli."; Mol. Microbiol. 22:21-29(1996).
[9]	ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-269, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan] Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.; "Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli."; Mol. Cell. Proteomics 0:0-0(2008).

Comments

CATALYTIC ACTIVITY: D-mannitol 1-phosphate + NAD⁺ = D-fructose 6-phosphate + NADH.
SUBUNIT: Monomer.
INTERACTION:
P0A821:selA; NbExp=1; IntAct=EBI-554652, EBI-1118693;
P77561:ydeP; NbExp=1; IntAct=EBI-554652, EBI-545210;
SIMILARITY: Belongs to the mannitol dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X51359; CAA35744.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00039; AAB18577.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76624.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77693.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X06794; CAA29954.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03845; AAA92661.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B65160; B65160.

RefSeq

AP_004192.1; -.
NP_418057.1; -.

3D structure databases

ModBase

P09424.

Protein-protein interaction databases

DIP

DIP:10268N; -.

IntAct

P09424; 11.

Enzyme and pathway databases

BioCyc

EcoCyc:MANNPDEHYDROG-MON; -.
MetaCyc:MANNPDEHYDROG-MON; -.

Organism-specific databases

EchoBASE

EB0611; -.

EcoGene

EG10616; mtlD.

Ontologies

GO:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0008926;	Molecular function: mannitol-1-phosphate 5-dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00196; -; 1.
PBIL [Tree]

InterPro

IPR013328; DHase_multihelical.
IPR013118; Mannitol_DHase_C.
IPR000669; Mannitol_DHase_core.
IPR013131; Mannitol_DHase_N.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

Pfam

PF01232; Mannitol_dh; 1.
PF08125; Mannitol_dh_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00084; MTLDHDRGNASE.

PROSITE

PS00974; MANNITOL_DHGENASE; 1.

Genome annotation databases

GeneID

948117; -.

GenomeReviews

AP009048_GR; JW3574.
U00096_GR; b3600.

KEGG

ecj:JW3574; -.
eco:b3600; -.

Phylogenomic databases

HOGENOM

P09424; -.

Genome annotation databases

CMR

P09424; b3600.

Other

ProtoNet

P09424.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Complete proteome; Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 382`	`382`	`Mannitol-1-phosphate 5-dehydrogenase.`	`PRO_0000170703`
`NP_BIND`	`3 14`	`12`	`NAD (By similarity).`
`MOD_RES`	`269 269`		`N6-acetyllysine.`
`CONFLICT`	`5 5`		`H -> V (in Ref. 8; AA sequence).`
`CONFLICT`	`14 15`		`GF -> SL (in Ref. 8; AA sequence).`
`CONFLICT`	`86 86`		`A -> R (in Ref. 1 and 2).`

Sequence information

Length: 382 AA [This is the length of the unprocessed precursor]

Molecular weight: 41139 Da [This is the MW of the unprocessed precursor]

CRC64: 1AC44028C150A7B2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKALHFGAGN IGRGFIGKLL ADAGIQLTFA DVNQVVLDAL NARHSYQVHV VGETEQVDTV 

        70         80         90        100        110        120 
SGVNAVSSIG DDVVDLIAQV DLVTTAVGPV VLERIAPAIA KGQVKRKEQG NESPLNIIAC 

       130        140        150        160        170        180 
ENMVRGTTQL KGHVMNALPE DAKAWVEEHV GFVDSAVDRI VPPSASATND PLEVTVETFS 

       190        200        210        220        230        240 
EWIVDKTQFK GALPNIPGME LTDNLMAFVE RKLFTLNTGH AITAYLGKLA GHQTIRDAIL 

       250        260        270        280        290        300 
DEKIRAVVKG AMEESGAVLI KRYGFDADKH AAYIQKILGR FENPYLKDDV ERVGRQPLRK 

       310        320        330        340        350        360 
LSAGDRLIKP LLGTLEYGLP HKNLIEGIAA AMHFRSEDDP QAQELAALIA DKGPQAALAQ 

       370        380 
ISGLDANSEV VSEAVTAYKA MQ

P09424 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools