Mannitol-1-phosphate 5-dehydrogenase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P09424 (MTLD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Mannitol-1-phosphate 5-dehydrogenase
EC=1.1.1.17

Gene names

Name:	mtlD
Ordered Locus Names:	b3600, JW3574

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-mannitol 1-phosphate + NAD⁺ = D-fructose 6-phosphate + NADH. HAMAP-Rule MF_00196
Subunit structure	Monomer.
Sequence similarities	Belongs to the mannitol dehydrogenase family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mannitol metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	coenzyme binding Inferred from electronic annotation. Source: InterPro mannitol-1-phosphate 5-dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
selA	P0A821	1	EBI-554652,EBI-1118693
ydeP	P77561	1	EBI-554652,EBI-545210

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 382

382

Mannitol-1-phosphate 5-dehydrogenase HAMAP-Rule MF_00196

PRO_0000170703

Regions

Nucleotide binding

3 – 14

NAD By similarity

Amino acid modifications

Modified residue

269

N6-acetyllysine Ref.9

Experimental info

Sequence conflict

H → V AA sequence Ref.8

Sequence conflict

14 – 15

GF → SL AA sequence Ref.8

Sequence conflict

A → R Ref.1

Sequence conflict

A → R Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P09424 [UniParc].

Last modified October 1, 1994. Version 3.
Checksum: 1AC44028C150A7B2
Show »

FASTA

382

41,139

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the mannitol (mtl) operon in Escherichia coli." Davis T., Yamada M., Elgort M., Saier M.H. Jr. Mol. Microbiol. 2:405-412(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Corrected sequence of the mannitol (mtl) operon in Escherichia coli." Jaiang W., Wu L.F., Tomich J., Saier M.H. Jr., Nichaus W.G. Mol. Microbiol. 4:2003-2006(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION. Strain: K12.
[3]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The mannitol repressor (MtlR) of Escherichia coli." Figge R.M., Ramseier T.M., Saier M.H. Jr. J. Bacteriol. 176:840-847(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 369-382. Strain: K12.
[7]	"Purification and properties of D-mannitol-1-phosphate dehydrogenase and D-glucitol-6-phosphate dehydrogenase from Escherichia coli." Novotny M.J., Reizer J., Esch F., Saier M.H. Jr. J. Bacteriol. 159:986-990(1984) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-25.
[8]	"FIS is a regulator of metabolism in Escherichia coli." Gonzalez-Gil G., Bringmann P., Kahmann R. Mol. Microbiol. 22:21-29(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15.
[9]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-269, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X51359 Genomic DNA. Translation: CAA35744.1. U00039 Genomic DNA. Translation: AAB18577.1. U00096 Genomic DNA. Translation: AAC76624.1. AP009048 Genomic DNA. Translation: BAE77693.1. X06794 Genomic DNA. Translation: CAA29954.1. Sequence problems. U03845 Genomic DNA. Translation: AAA92661.1.
PIR	B65160.
RefSeq	NP_418057.1. NC_000913.2. YP_491834.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P09424.
SMR	P09424. Positions 1-382.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10268N.
IntAct	P09424. 11 interactions.
MINT	MINT-1240338.
STRING	511145.b3600.
Proteomic databases
PaxDb	P09424.
PRIDE	P09424.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76624; AAC76624; b3600. BAE77693; BAE77693; BAE77693.
GeneID	12932279. 948117.
KEGG	ecj:Y75_p3575. eco:b3600.
PATRIC	32122683. VBIEscCol129921_3718.
Organism-specific databases
EchoBASE	EB0611.
EcoGene	EG10616. mtlD.
Phylogenomic databases
eggNOG	COG0246.
HOGENOM	HOG000271391.
KO	K00009.
OMA	GHATTAY.
ProtClustDB	PRK02318.
Enzyme and pathway databases
BioCyc	EcoCyc:MANNPDEHYDROG-MONOMER. ECOL316407:JW3574-MONOMER. MetaCyc:MANNPDEHYDROG-MONOMER.
Gene expression databases
Genevestigator	P09424.
Family and domain databases
Gene3D	1.10.1040.10. 1 hit. 3.40.50.720. 1 hit.
HAMAP	MF_00196. Mannitol_dehydrog.
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR013328. DH_multihelical. IPR023028. Mannitol_1_phos_5_DH. IPR000669. Mannitol_DH. IPR013118. Mannitol_DH_C. IPR023027. Mannitol_DH_CS. IPR013131. Mannitol_DH_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF01232. Mannitol_dh. 1 hit. PF08125. Mannitol_dh_C. 1 hit. [Graphical view]
PRINTS	PR00084. MTLDHDRGNASE.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
PROSITE	PS00974. MANNITOL_DHGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MTLD_ECOLI

Accession

Primary (citable) accession number: P09424
Secondary accession number(s): Q2M7R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1994
Last modified:	May 29, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents