UniProtKB - P45425 (NANK_ECOLI)
Protein
N-acetylmannosamine kinase
Gene
nanK
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. Has also low level glucokinase activity in vitro.2 Publications
Catalytic activityi
- EC:2.7.1.60
Kineticsi
Catalytic efficiency with N-acyl-D-mannosamine as substrate is 136-fold higher than that with D-glucose.
- KM=0.36 mM for N-acyl-D-mannosamine (at 25 degrees Celsius and pH 7.6)2 Publications
- KM=0.26 mM for ATP (at 25 degrees Celsius and pH 7.6)2 Publications
- KM=20 mM for D-glucose (at 25 degrees Celsius and pH 7.6)2 Publications
- KM=84 mM for D-mannose (at 25 degrees Celsius and pH 7.6)2 Publications
: N-acetylneuraminate degradation Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.Proteins known to be involved in the 5 steps of the subpathway in this organism are:
- N-acetylneuraminate lyase (nanA), N-acetylneuraminate lyase (nanA)
- N-acetylmannosamine kinase (nanK), N-acetylmannosamine kinase (nanK)
- Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE), Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
- N-acetylglucosamine-6-phosphate deacetylase (nagA)
- Glucosamine-6-phosphate deaminase (nagB), Glucosamine-6-phosphate deaminase (nagB)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate, the pathway N-acetylneuraminate degradation and in Amino-sugar metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 156 | Zinc | 1 | |
Metal bindingi | 166 | Zinc | 1 | |
Metal bindingi | 168 | Zinc | 1 | |
Metal bindingi | 173 | Zinc | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 5 – 12 | ATPSequence analysis | 8 | |
Nucleotide bindingi | 132 – 139 | ATPSequence analysis | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-UniRule
- N-acylmannosamine kinase activity Source: EcoCyc
- zinc ion binding Source: UniProtKB-UniRule
GO - Biological processi
- cellular response to DNA damage stimulus Source: EcoliWiki
- N-acetylmannosamine metabolic process Source: UniProtKB-UniRule
- N-acetylneuraminate catabolic process Source: EcoCyc
Keywordsi
Molecular function | Kinase, Transferase |
Biological process | Carbohydrate metabolism |
Ligand | ATP-binding, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BioCyci | EcoCyc:NANK-MONOMER MetaCyc:NANK-MONOMER |
SABIO-RKi | P45425 |
UniPathwayi | UPA00629;UER00681 |
Names & Taxonomyi
Protein namesi | Recommended name: N-acetylmannosamine kinase (EC:2.7.1.60)Alternative name(s): ManNAc kinase N-acetyl-D-mannosamine kinase |
Gene namesi | Name:nanK Synonyms:yhcI Ordered Locus Names:b3222, JW5538 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 84 | L → P: 12-fold increase in catalytic efficiency for glucose phosphorylation. 2-fold decrease in catalytic efficiency for N-acetylmannosamine phosphorylation. 1 Publication | 1 | |
Mutagenesisi | 138 | V → M: 6-fold increase in catalytic efficiency for glucose phosphorylation. No change in catalytic efficiency for N-acetylmannosamine phosphorylation. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000095695 | 1 – 291 | N-acetylmannosamine kinaseAdd BLAST | 291 |
Proteomic databases
jPOSTi | P45425 |
PaxDbi | P45425 |
PRIDEi | P45425 |
Expressioni
Inductioni
Negatively regulated by the transcriptional repressor NanR. Induced by N-acetylneuraminate, via inactivation of NanR.1 Publication
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4261227, 316 interactors |
DIPi | DIP-12282N |
IntActi | P45425, 1 interactor |
STRINGi | 511145.b3222 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P45425 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P45425 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1940, Bacteria |
HOGENOMi | CLU_036604_0_4_6 |
InParanoidi | P45425 |
PhylomeDBi | P45425 |
Family and domain databases
HAMAPi | MF_01234, ManNAc_kinase, 1 hit |
InterProi | View protein in InterPro IPR043129, ATPase_NBD IPR023945, ManNAc_kinase_bac IPR000600, ROK |
PANTHERi | PTHR18964, PTHR18964, 1 hit |
Pfami | View protein in Pfam PF00480, ROK, 1 hit |
SUPFAMi | SSF53067, SSF53067, 1 hit |
PROSITEi | View protein in PROSITE PS01125, ROK, 1 hit |
i Sequence
Sequence statusi: Complete.
P45425-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTTLAIDIGG TKLAAALIGA DGQIRDRREL PTPASQTPEA LRDALSALVS
60 70 80 90 100
PLQAHAQRVA IASTGIIRDG SLLALNPHNL GGLLHFPLVK TLEQLTNLPT
110 120 130 140 150
IAINDAQAAA WAEFQALDGD ITDMVFITVS TGVGGGVVSG CKLLTGPGGL
160 170 180 190 200
AGHIGHTLAD PHGPVCGCGR TGCVEAIASG RGIAAAAQGE LAGADAKTIF
210 220 230 240 250
TRAGQGDEQA QQLIHRSART LARLIADIKA TTDCQCVVVG GSVGLAEGYL
260 270 280 290
ALVETYLAQE PAAFHVDLLA AHYRHDAGLL GAALLAQGEK L
Sequence cautioni
The sequence AAA58024 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U18997 Genomic DNA Translation: AAA58024.1 Different initiation. U00096 Genomic DNA Translation: AAC76254.2 AP009048 Genomic DNA Translation: BAE77265.1 |
PIRi | H65113 |
RefSeqi | NP_417689.4, NC_000913.3 WP_000209011.1, NZ_SSZK01000034.1 |
Genome annotation databases
EnsemblBacteriai | AAC76254; AAC76254; b3222 BAE77265; BAE77265; BAE77265 |
GeneIDi | 947757 |
KEGGi | ecj:JW5538 eco:b3222 |
PATRICi | fig|1411691.4.peg.3506 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U18997 Genomic DNA Translation: AAA58024.1 Different initiation. U00096 Genomic DNA Translation: AAC76254.2 AP009048 Genomic DNA Translation: BAE77265.1 |
PIRi | H65113 |
RefSeqi | NP_417689.4, NC_000913.3 WP_000209011.1, NZ_SSZK01000034.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2AA4 | X-ray | 2.20 | A/B | 1-289 | [»] | |
SMRi | P45425 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261227, 316 interactors |
DIPi | DIP-12282N |
IntActi | P45425, 1 interactor |
STRINGi | 511145.b3222 |
Proteomic databases
jPOSTi | P45425 |
PaxDbi | P45425 |
PRIDEi | P45425 |
Genome annotation databases
EnsemblBacteriai | AAC76254; AAC76254; b3222 BAE77265; BAE77265; BAE77265 |
GeneIDi | 947757 |
KEGGi | ecj:JW5538 eco:b3222 |
PATRICi | fig|1411691.4.peg.3506 |
Organism-specific databases
EchoBASEi | EB2666 |
Phylogenomic databases
eggNOGi | COG1940, Bacteria |
HOGENOMi | CLU_036604_0_4_6 |
InParanoidi | P45425 |
PhylomeDBi | P45425 |
Enzyme and pathway databases
UniPathwayi | UPA00629;UER00681 |
BioCyci | EcoCyc:NANK-MONOMER MetaCyc:NANK-MONOMER |
SABIO-RKi | P45425 |
Miscellaneous databases
EvolutionaryTracei | P45425 |
PROi | PR:P45425 |
Family and domain databases
HAMAPi | MF_01234, ManNAc_kinase, 1 hit |
InterProi | View protein in InterPro IPR043129, ATPase_NBD IPR023945, ManNAc_kinase_bac IPR000600, ROK |
PANTHERi | PTHR18964, PTHR18964, 1 hit |
Pfami | View protein in Pfam PF00480, ROK, 1 hit |
SUPFAMi | SSF53067, SSF53067, 1 hit |
PROSITEi | View protein in PROSITE PS01125, ROK, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NANK_ECOLI | |
Accessioni | P45425Primary (citable) accession number: P45425 Secondary accession number(s): Q2M8Z1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | December 15, 1998 | |
Last modified: | April 7, 2021 | |
This is version 140 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- 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