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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Escherichia coli K-12 substr. MG1655 Enzyme: N-acetylmannosamine kinase



Gene: nanK Accession Numbers: G7676 (EcoCyc), b3222, ECK3211

Synonyms: yhcI

Regulation Summary Diagram: ?

Summary:
NanK belongs to the family of ROK sugar kinases [Plumbridge99, Larion07] and was shown to have both N-acetylmannosamine kinase and rudimentary glucokinase activity in vitro [Miller04a].

Overexpression of nanK rescues the glucose auxotrophy of a glucokinase mutant [Miller04a].

Transcription of the nanATEK-yhcH (sialic acid catabolic) operon is repressed by NanR [Kalivoda03].

Gene Citations: [Ohta85, Kalivoda13]

Locations: cytosol

Map Position: [3,367,497 <- 3,368,372] (72.58 centisomes)
Length: 876 bp / 291 aa

Molecular Weight of Polypeptide: 29.644 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0010571 , DIP:DIP-12282N , EchoBASE:EB2666 , EcoGene:EG12815 , EcoliWiki:b3222 , ModBase:P45425 , OU-Microarray:b3222 , PortEco:nanK , PR:PRO_000023342 , Pride:P45425 , Protein Model Portal:P45425 , RefSeq:NP_417689 , RegulonDB:G7676 , SMR:P45425 , String:511145.b3222 , UniProt:P45425

Relationship Links: InterPro:IN-FAMILY:IPR000600 , InterPro:IN-FAMILY:IPR023945 , PDB:Structure:2AA4 , Pfam:IN-FAMILY:PF00480 , Prosite:IN-FAMILY:PS01125

In Paralogous Gene Group: 118 (7 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0019262 - N-acetylneuraminate catabolic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, GOA01, Hopkins13, Miller04a]
GO:0046835 - carbohydrate phosphorylation Inferred by computational analysis Inferred from experiment [Miller04a, GOA06, GOA01a, GOA01]
GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0006051 - N-acetylmannosamine metabolic process Inferred by computational analysis [GOA06]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0009384 - N-acylmannosamine kinase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Miller04a]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0008270 - zinc ion binding Inferred by computational analysis [GOA06, GOA01]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005737 - cytoplasm
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism central intermediary metabolism amino sugar conversions

Essentiality data for nanK knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 23-Apr-2008 by Keseler I , SRI International


Enzymatic reaction of: N-acetylmannosamine kinase

Synonyms: ManNAc kinase

EC Number: 2.7.1.60

N-acetyl-D-mannosamine + ATP <=> N-acetyl-D-mannosamine 6-phosphate + ADP + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for N-acetyl-D-mannosamine: D-glucose [Larion07 ] , D-mannose [Larion07 ]

In Pathways: superpathway of N-acetylglucosamine, N-acetylmannosamine and N-acetylneuraminate degradation , N-acetylneuraminate and N-acetylmannosamine degradation

Summary:
The enzyme from Salmonella typhimurium has been purified and characterized [Banerjee69]. Cloning and overexpression of nanK from E. coli K1 also yielded active enzyme [Ringenberg03].

Kinetic Parameters:

Substrate
Km (μM)
Citations
ATP
510.0
[Miller04a]


Sequence Features

Feature Class Location Citations Comment
Nucleotide-Phosphate-Binding-Region 5 -> 12
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 84
[Larion07, UniProt11]
Alternate sequence: L → P; UniProt: 12-fold increase in catalytic efficiency for glucose phosphorylation. 2-fold decrease in catalytic efficiency for N-acetylmannosamine phosphorylation.
Nucleotide-Phosphate-Binding-Region 132 -> 139
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 138
[Larion07, UniProt11]
Alternate sequence: V → M; UniProt: 6-fold increase in catalytic efficiency for glucose phosphorylation. No change in catalytic efficiency for N- acetylmannosamine phosphorylation.
Metal-Binding-Site 156
[UniProt10]
UniProt: Zinc;
Metal-Binding-Site 166
[UniProt10]
UniProt: Zinc;
Metal-Binding-Site 168
[UniProt10]
UniProt: Zinc;
Metal-Binding-Site 173
[UniProt10]
UniProt: Zinc;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
Ingrid Keseler on Tue Jul 23, 2013:
The start site of this gene was originally assigned solely on the basis of sequence considerations [Blattner97 ]. However, it was changed because Miller et al [Miller04a ] attested that the real start site is actually located 33 bp downstream and its ATG start codon was re-annotated at the 3368372 position. The demonstration is based on sequence analysis. This information was obtained from the EcoGene database (http://bmb.med.miami.edu/EcoGene/EcoWeb/).


Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Banerjee69: Banerjee S, Ghosh S (1969). "Purification and properties of N-acetylmannosamine kinase from Salmonella typhimurium." Eur J Biochem 8(2);200-6. PMID: 4889177

Blattner97: Blattner FR, Plunkett G, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y (1997). "The complete genome sequence of Escherichia coli K-12." Science 277(5331);1453-74. PMID: 9278503

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Hopkins13: Hopkins AP, Hawkhead JA, Thomas GH (2013). "Transport and catabolism of the sialic acids N-glycolylneuraminic acid and 3-keto-3-deoxy-D-glycero-D-galactonononic acid by Escherichia coli K-12." FEMS Microbiol Lett 347(1);14-22. PMID: 23848303

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kalivoda03: Kalivoda KA, Steenbergen SM, Vimr ER, Plumbridge J (2003). "Regulation of sialic acid catabolism by the DNA binding protein NanR in Escherichia coli." J Bacteriol 185(16);4806-15. PMID: 12897000

Kalivoda13: Kalivoda KA, Steenbergen SM, Vimr ER (2013). "Control of the Escherichia coli sialoregulon by transcriptional repressor NanR." J Bacteriol 195(20);4689-701. PMID: 23935044

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Larion07: Larion M, Moore LB, Thompson SM, Miller BG (2007). "Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity." Biochemistry 46(47);13564-72. PMID: 17979299

Miller04a: Miller BG, Raines RT (2004). "Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases." Biochemistry 43(21);6387-92. PMID: 15157072

Ohta85: Ohta Y, Watanabe K, Kimura A (1985). "Complete nucleotide sequence of the E. coli N-acetylneuraminate lyase." Nucleic Acids Res 13(24);8843-52. PMID: 3909108

Plumbridge99: Plumbridge J, Vimr E (1999). "Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli." J Bacteriol 1999;181(1);47-54. PMID: 9864311

Ringenberg03: Ringenberg MA, Steenbergen SM, Vimr ER (2003). "The first committed step in the biosynthesis of sialic acid by Escherichia coli K1 does not involve a phosphorylated N-acetylmannosamine intermediate." Mol Microbiol 50(3);961-75. PMID: 14617154

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Other References Related to Gene Regulation

Beisel11: Beisel CL, Storz G (2011). "The base-pairing RNA spot 42 participates in a multioutput feedforward loop to help enact catabolite repression in Escherichia coli." Mol Cell 41(3);286-97. PMID: 21292161

Beisel12: Beisel CL, Updegrove TB, Janson BJ, Storz G (2012). "Multiple factors dictate target selection by Hfq-binding small RNAs." EMBO J 31(8);1961-74. PMID: 22388518

Bradley07: Bradley MD, Beach MB, de Koning AP, Pratt TS, Osuna R (2007). "Effects of Fis on Escherichia coli gene expression during different growth stages." Microbiology 153(Pt 9);2922-40. PMID: 17768236


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc13.