Reviewed, UniProtKB/Swiss-Prot P09424 (MTLD_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	D-mannitol 1-phosphate + NAD(+) = D-fructose 6-phosphate + NADH.
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
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	coenzyme binding Inferred from electronic annotation. Source: InterPro mannitol-1-phosphate 5-dehydrogenase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
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		PRO_0000170703
Regions
	Nucleotide binding	3 – 14	12	NAD By similarity
Amino acid modifications
	Modified residue	269	1	N6-acetyllysine
Experimental info
	Sequence conflict	5	1	H → V AA sequence Ref.8
	Sequence conflict	14 – 15	2	GF → SL AA sequence Ref.8
	Sequence conflict	86	1	A → R Ref.1 Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P09424-1 [UniParc]. Last modified October 1, 1994. Version 3. Checksum: 1AC44028C150A7B2	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

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: 3135464] [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: 1964486] [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: 8041620] [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: 9278503] [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: 16738553] [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: 8300537] [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: 6384188] [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: 8899705] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15.
[9]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 0:0-0(2008) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-269, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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	AP_004192.1. NP_418057.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:10268N.
IntAct	P09424.
Genome annotation databases
GeneID	948117.
GenomeReviews	Gene locus b3600 in contig U00096_GR. Gene locus JW3574 in contig AP009048_GR.
KEGG	ecj:JW3574. eco:b3600.
Organism-specific databases
EchoBASE	EB0611.
EcoGene	EG10616. mtlD.
CMR	Search...
Phylogenomic databases
HOGENOM	P09424.
Enzyme and pathway databases
BioCyc	EcoCyc:MANNPDEHYDROG-MON. MetaCyc:MANNPDEHYDROG-MON.
Family and domain databases
HAMAP	MF_00196. [Tree]
InterPro	IPR013328. DHase_multihelical. IPR013118. Mannitol_DHase_C. IPR000669. Mannitol_DHase_core. IPR013131. Mannitol_DHase_N. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
Pfam	PF01232. Mannitol_dh. 1 hit. PF08125. Mannitol_dh_C. 1 hit. [Graphical view]
PRINTS	PR00084. MTLDHDRGNASE.
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:	November 25, 2008
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)