N-acetylmannosamine kinase - Escherichia coli (strain K12)

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P45425 (NANK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
N-acetylmannosamine kinase
EC=2.7.1.60

Alternative name(s):
ManNAc kinase
N-acetyl-D-mannosamine kinase

Gene names

Name:	nanK
Synonyms:	yhcI
Ordered Locus Names:	b3222, JW5538

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	291 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. Has also low level glucokinase activity in vitro. Ref.3 Ref.4 Ref.5
Catalytic activity	ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate. HAMAP-Rule MF_01234
Pathway	Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 2/5. HAMAP-Rule MF_01234
Subunit structure	Homodimer. Ref.6
Sequence similarities	Belongs to the ROK (NagC/XylR) family. NanK subfamily.
Biophysicochemical properties	Kinetic parameters: Catalytic efficiency with N-acyl-D-mannosamine as substrate is 136-fold higher than that with D-glucose. K_M=0.36 mM for N-acyl-D-mannosamine (at 25 degrees Celsius and pH 7.6) Ref.4 Ref.5 K_M=0.26 mM for ATP (at 25 degrees Celsius and pH 7.6) K_M=20 mM for D-glucose (at 25 degrees Celsius and pH 7.6) K_M=84 mM for D-mannose (at 25 degrees Celsius and pH 7.6)
Sequence caution	The sequence AAA58024.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-acetylmannosamine metabolic process Inferred from electronic annotation. Source: HAMAP N-acetylneuraminate catabolic process Inferred from direct assay Ref.4. Source: EcoCyc response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP N-acylmannosamine kinase activity Inferred from direct assay Ref.4. Source: EcoCyc zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 291

291

N-acetylmannosamine kinase HAMAP-Rule MF_01234

PRO_0000095695

Regions

Nucleotide binding

5 – 12

ATP Potential

Nucleotide binding

132 – 139

ATP Potential

Sites

Metal binding

156

Zinc

Metal binding

166

Zinc

Metal binding

168

Zinc

Metal binding

173

Zinc

Experimental info

Mutagenesis

L → P: 12-fold increase in catalytic efficiency for glucose phosphorylation. 2-fold decrease in catalytic efficiency for N-acetylmannosamine phosphorylation. Ref.5

Mutagenesis

138

V → M: 6-fold increase in catalytic efficiency for glucose phosphorylation. No change in catalytic efficiency for N-acetylmannosamine phosphorylation. Ref.5

Secondary structure

291

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P45425 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: E3109E2756B08612
Show »

FASTA

291

29,644

        10         20         30         40         50         60 
MTTLAIDIGG TKLAAALIGA DGQIRDRREL PTPASQTPEA LRDALSALVS PLQAHAQRVA 

        70         80         90        100        110        120 
IASTGIIRDG SLLALNPHNL GGLLHFPLVK TLEQLTNLPT IAINDAQAAA WAEFQALDGD 

       130        140        150        160        170        180 
ITDMVFITVS TGVGGGVVSG CKLLTGPGGL AGHIGHTLAD PHGPVCGCGR TGCVEAIASG 

       190        200        210        220        230        240 
RGIAAAAQGE LAGADAKTIF TRAGQGDEQA QQLIHRSART LARLIADIKA TTDCQCVVVG 

       250        260        270        280        290 
GSVGLAEGYL ALVETYLAQE PAAFHVDLLA AHYRHDAGLL GAALLAQGEK L

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli." Plumbridge J., Vimr E. J. Bacteriol. 181:47-54(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PUTATIVE FUNCTION.
[4]	"Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases." Miller B.G., Raines R.T. Biochemistry 43:6387-6392(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, KINETIC PARAMETERS. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[5]	"Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity." Larion M., Moore L.B., Thompson S.M., Miller B.G. Biochemistry 46:13564-13572(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, MUTAGENESIS OF LEU-84 AND VAL-138.
[6]	"Crystal structure of Escherichia coli putative N-acetylmannosamine kinase." New York structural genomics research consortium (NYSGRC) Submitted (JUL-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-289 IN COMPLEX WITH ZINC IONS, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U18997 Genomic DNA. Translation: AAA58024.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76254.2.
AP009048 Genomic DNA. Translation: BAE77265.1.

PIR

H65113.

RefSeq

NP_417689.4. NC_000913.2.
YP_491406.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AA4	X-ray	2.20	A/B	1-289	[»]

ProteinModelPortal

P45425.

SMR

P45425. Positions 1-289.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-12282N.

IntAct

P45425. 1 interaction.

STRING

511145.b3222.

Proteomic databases

PRIDE

P45425.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76254; AAC76254; b3222.
BAE77265; BAE77265; BAE77265.

GeneID

12932233.
947757.

KEGG

ecj:Y75_p3142.
eco:b3222.

PATRIC

32121868. VBIEscCol129921_3318.

Organism-specific databases

EchoBASE

EB2666.

EcoGene

EG12815. nanK.

Phylogenomic databases

eggNOG

COG1940.

HOGENOM

HOG000150087.

K00885.

OMA

DITEMVF.

ProtClustDB

PRK05082.

Enzyme and pathway databases

BioCyc

EcoCyc:NANK-MONOMER.
ECOL316407:JW5538-MONOMER.
MetaCyc:NANK-MONOMER.

SABIO-RK

P45425.

UniPathway

UPA00629; UER00681.

Gene expression databases

Genevestigator

P45425.

Family and domain databases

HAMAP

MF_01234. ManNAc_kinase.

InterPro

IPR023945. ManNAc_kinase_bac.
IPR000600. ROK.
[Graphical view]

Pfam

PF00480. ROK. 1 hit.
[Graphical view]

PROSITE

PS01125. ROK. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P45425.

Entry information

Entry name

NANK_ECOLI

Accession

Primary (citable) accession number: P45425
Secondary accession number(s): Q2M8Z1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	December 15, 1998
Last modified:	May 1, 2013
This is version 97 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

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

Other

Entry information

Relevant documents