UniProtKB - P0AF18 (NAGA_ECOLI)

BLAST

>sp|P0AF18|NAGA_ECOLI N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=nagA PE=1 SV=1
MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQL
NGCGGVQFNDTAEAVSVETLEIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLAK
HPNQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLCENADVITKVTLAPEMVPAEV
ISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEAD
IYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCV
DENGTLSGSSLTMIEGVRNLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANL
TAFTPDFKITKTIVNGNEVVTQ

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History
Entry version 101 (10 Oct 2018)
Sequence version 1 (20 Dec 2005)
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Protein

N-acetylglucosamine-6-phosphate deacetylase

Gene

nagA

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Involved in the first step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate. In vitro, can also hydrolyze substrate analogs such as N-thioacetyl-D-glucosamine-6-phosphate, N-trifluoroacetyl-D-glucosamine-6-phosphate, N-acetyl-D-glucosamine-6-sulfate, N-acetyl-D-galactosamine-6-phosphate, and N-formyl-D-glucosamine-6-phosphate.6 Publications

Manual assertion based on experiment inⁱ

Ref.2
"Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli."
Peri K.G., Goldie H., Waygood E.B.
Biochem. Cell Biol. 68:123-137(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Ref.6
"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Ref.8
"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM.
Ref.11
"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM.
Ref.12
"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT.
Ref.13
"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.

Catalytic activityⁱ

N-acetyl-D-glucosamine 6-phosphate + H₂O = D-glucosamine 6-phosphate + acetate.5 Publications

Cofactorⁱ

Zn²⁺3 Publications, Co²⁺3 Publications, Mn²⁺3 Publications, Cd²⁺3 Publications, Fe²⁺3 Publications, Ni²⁺3 PublicationsNote: Binds 1 divalent metal cation per subunit. The highest efficient metals are Zn²⁺ and Co²⁺, followed by Mn²⁺, Cd²⁺, Fe²⁺ and Ni²⁺.3 Publications

Activity regulationⁱ

Inhibited by high substrate concentration and by products glucosamine 6-phosphate and acetate. Completely inactivated by the treatment with 5,5'-dithio-bis(2-nitrobenzoate) or 2,2'-dithio-pyridine (2-DPDS). Inhibited by 1,10-phenanthroline and EDTA.4 Publications

Kineticsⁱ

kcat is 102 sec(-1) for the deacetylation of N-acetyl-D-glucosamine-6-phosphate by the Zn-enzyme. The Cd-NagA catalyzes the hydrolysis of N-thioacetyl-D-glucosamine-6-phosphate substrate about an order of magnitude better than does the Zn-substituted enzyme. The N-trifluoroacetyl substituted substrate is hydrolyzed 26 times faster than the natural substrate, but the N-formyl substrate is hydrolyzed more slowly by a factor of 5.3 Publications

pH dependenceⁱ

Optimum pH is 8.5.3 Publications

Pathwayⁱ: N-acetylneuraminate degradation

This protein is involved in step 4 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.1 Publication
Proteins known to be involved in the 5 steps of the subpathway in this organism are:

N-acetylneuraminate lyase (nanA)
N-acetylmannosamine kinase (nanK)
Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
N-acetylglucosamine-6-phosphate deacetylase (nagA)
Glucosamine-6-phosphate deaminase (nagB)

This subpathway is part of the pathway N-acetylneuraminate degradation, which is itself part of Amino-sugar metabolism.
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	Length
Metal bindingⁱ	131	Zinc1 Publication	1
Metal bindingⁱ	195	Zinc; via tele nitrogen1 Publication	1
Metal bindingⁱ	216	Zinc; via tele nitrogen1 Publication	1
Binding siteⁱ	227	Substrate1 Publication	1
Active siteⁱ	273	Proton donor/acceptor1 Publication	1

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Carbohydrate metabolism
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	EcoCyc:NAG6PDEACET-MONOMER MetaCyc:NAG6PDEACET-MONOMER
BRENDAⁱ	3.5.1.25 2026
SABIO-RKⁱ	P0AF18
UniPathwayⁱ	UPA00629;UER00683

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: N-acetylglucosamine-6-phosphate deacetylase1 Publication (EC:3.5.1.255 Publications) Short name: GlcNAc 6-P deacetylase1 Publication
Gene namesⁱ	Name:nagA Ordered Locus Names:b0677, JW0663
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10632 nagA

EcoGeneⁱ

EG10632 nagA

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Synthesizes high levels of glucosamine-6-phosphate deaminase and over half of the amount of glucosamine-6-phosphate synthase compared to wild-type.1 Publication

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	59	Q → H: Large decrease in catalytic activity and substrate affinity, and increase in the average amount of Zn bound to the protein, suggesting that an additional metal ion can bind to this mutant; when associated with H-61. 2 Publications	1
Mutagenesisⁱ	61	N → H: Large decrease in catalytic activity and substrate affinity, and increase in the average amount of Zn bound to the protein, suggesting that an additional metal ion can bind to this mutant; when associated with H-59. 1 Publication	1
Mutagenesisⁱ	131	E → Q or A: Large reduction in the amount of the metal cofactor bound to the enzyme. 1 Publication	1
Mutagenesisⁱ	143	H → N: Dramatic decrease in catalytic activity and moderate decrease in substrate affinity, producing a 6000-fold decrease in catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	143	H → Q: 180-fold decrease in catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	251	H → N: 500-fold decrease in catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	273	D → N or A: Loss of catalytic activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000170915	1 – 382	N-acetylglucosamine-6-phosphate deacetylaseAdd BLAST		382

Proteomic databases

EPDⁱ	P0AF18
PaxDbⁱ	P0AF18
PRIDEⁱ	P0AF18

Expressionⁱ

Inductionⁱ

By N-acetylglucosamine. Induced by low extracellular levels of magnesium via the PhoQ/PhoP two-component regulatory system.1 Publication

Interactionⁱ

Subunit structureⁱ

Homotetramer.4 Publications

Protein-protein interaction databases

BioGridⁱ	4261208, 26 interactors
Database of interacting proteins More...DIPⁱ	DIP-10297N
IntActⁱ	P0AF18, 5 interactors
STRINGⁱ	316385.ECDH10B_0742

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	2 – 10	Combined sources	9
Beta strandⁱ	15 – 24	Combined sources	10
Beta strandⁱ	27 – 33	Combined sources	7
Helixⁱ	34 – 36	Combined sources	3
Beta strandⁱ	43 – 45	Combined sources	3
Beta strandⁱ	50 – 53	Combined sources	4
Beta strandⁱ	55 – 63	Combined sources	9
Beta strandⁱ	66 – 71	Combined sources	6
Turnⁱ	72 – 74	Combined sources	3
Helixⁱ	77 – 89	Combined sources	13
Beta strandⁱ	92 – 100	Combined sources	9
Helixⁱ	104 – 120	Combined sources	17
Beta strandⁱ	123 – 125	Combined sources	3
Beta strandⁱ	128 – 131	Combined sources	4
Helixⁱ	137 – 139	Combined sources	3
Helixⁱ	145 – 147	Combined sources	3
Helixⁱ	150 – 161	Combined sources	12
Turnⁱ	162 – 165	Combined sources	4
Beta strandⁱ	166 – 171	Combined sources	6
Helixⁱ	173 – 175	Combined sources	3
Helixⁱ	178 – 186	Combined sources	9
Beta strandⁱ	190 – 193	Combined sources	4
Helixⁱ	200 – 209	Combined sources	10
Beta strandⁱ	213 – 216	Combined sources	4
Turnⁱ	217 – 220	Combined sources	4
Helixⁱ	230 – 237	Combined sources	8
Beta strandⁱ	242 – 246	Combined sources	5
Beta strandⁱ	248 – 252	Combined sources	5
Helixⁱ	254 – 264	Combined sources	11
Helixⁱ	265 – 267	Combined sources	3
Beta strandⁱ	268 – 271	Combined sources	4
Turnⁱ	276 – 279	Combined sources	4
Beta strandⁱ	283 – 287	Combined sources	5
Beta strandⁱ	290 – 294	Combined sources	5
Beta strandⁱ	298 – 301	Combined sources	4
Beta strandⁱ	306 – 309	Combined sources	4
Helixⁱ	313 – 324	Combined sources	12
Helixⁱ	328 – 335	Combined sources	8
Helixⁱ	337 – 342	Combined sources	6
Turnⁱ	346 – 348	Combined sources	3
Beta strandⁱ	349 – 351	Combined sources	3
Beta strandⁱ	360 – 363	Combined sources	4
Beta strandⁱ	369 – 374	Combined sources	6
Beta strandⁱ	377 – 381	Combined sources	5

Show more details

3D structure databases

ProteinModelPortalⁱ	P0AF18
SMRⁱ	P0AF18
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0AF18

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	142 – 143	Substrate binding1 Publication	2
Regionⁱ	219 – 220	Substrate binding1 Publication	2
Regionⁱ	248 – 251	Substrate binding1 Publication	4
Regionⁱ	306 – 308	Substrate binding1 Publication	3

Sequence similaritiesⁱ

Belongs to the metallo-dependent hydrolases superfamily. NagA family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105CE4 Bacteria COG1820 LUCA
HOGENOMⁱ	HOG000275008
InParanoidⁱ	P0AF18
KEGG Orthology (KO) More...KOⁱ	K01443
OMAⁱ	HAFNAMP
PhylomeDBⁱ	P0AF18

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00854 NagA, 1 hit
Gene3Dⁱ	2.30.40.10, 2 hits
InterProⁱ	View protein in InterPro IPR006680 Amidohydro-rel IPR003764 GlcNAc_6-P_deAcase IPR011059 Metal-dep_hydrolase_composite IPR032466 Metal_Hydrolase
PANTHERⁱ	PTHR11113:SF1 PTHR11113:SF1, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01979 Amidohydro_1, 1 hit
PIRSFⁱ	PIRSF038994 NagA, 1 hit
SUPFAMⁱ	SSF51338 SSF51338, 1 hit SSF51556 SSF51556, 1 hit
TIGRFAMsⁱ	TIGR00221 nagA, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0AF18-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MYALTQGRIF TGHEFLDDHA VVIADGLIKS VCPVAELPPE IEQRSLNGAI 
        60         70         80         90        100
LSPGFIDVQL NGCGGVQFND TAEAVSVETL EIMQKANEKS GCTNYLPTLI 
       110        120        130        140        150
TTSDELMKQG VRVMREYLAK HPNQALGLHL EGPWLNLVKK GTHNPNFVRK 
       160        170        180        190        200
PDAALVDFLC ENADVITKVT LAPEMVPAEV ISKLANAGIV VSAGHSNATL 
       210        220        230        240        250
KEAKAGFRAG ITFATHLYNA MPYITGREPG LAGAILDEAD IYCGIIADGL 
       260        270        280        290        300
HVDYANIRNA KRLKGDKLCL VTDATAPAGA NIEQFIFAGK TIYYRNGLCV 
       310        320        330        340        350
DENGTLSGSS LTMIEGVRNL VEHCGIALDE VLRMATLYPA RAIGVEKRLG 
       360        370        380 
TLAAGKVANL TAFTPDFKIT KTIVNGNEVV TQ

Length:382

Mass (Da):40,949

Last modified:December 20, 2005 - v1

Checksum:ⁱA10B015ADFC98FCA

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X14135 Genomic DNA Translation: CAA32353.1 AF052007 Genomic DNA Translation: AAC09325.1 U00096 Genomic DNA Translation: AAC73771.1 AP009048 Genomic DNA Translation: BAA35320.1
PIRⁱ	A37018
NCBI Reference Sequences More...RefSeqⁱ	NP_415203.1, NC_000913.3 WP_000271153.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73771; AAC73771; b0677 BAA35320; BAA35320; BAA35320
GeneIDⁱ	945289
KEGGⁱ	ecj:JW0663 eco:b0677
PATRICⁱ	fig\|1411691.4.peg.1601

Protein	Similar proteins		Species	Score	Length	Source
P0AF18	N-acetylglucosamine-6-phosphate deacetylase		ECO57		382	UniRef100_P0AF19
N-acetylglucosamine-6-phosphate deacetylase		Escherichia coli B354		397
N-acetylglucosamine-6-phosphate deacetylase		Escherichia coli O145 str. RM9872		382
N-acetylglucosamine-6-phosphate deacetylase		KLEPN		382
N-acetylglucosamine-6-phosphate deacetylase		uncultured bacterium Contig1417		382
+62

Protein	Similar proteins		Species	Score	Length	Source
P0AF18	N-acetylglucosamine-6-phosphate deacetylase		ECO57		382	UniRef90_P0AF19
N-acetylglucosamine-6-phosphate deacetylase		Escherichia coli B354		397
N-acetylglucosamine-6-phosphate deacetylase		Escherichia coli O145 str. RM9872		382
N-acetylglucosamine-6-phosphate deacetylase		KLEPN		382
N-acetylglucosamine-6-phosphate deacetylase		uncultured bacterium Contig1417		382
+536

Protein	Similar proteins		Species	Score	Length	Source
P0AF18	N-acetylglucosamine-6-phosphate deacetylase		ECO57		382	UniRef50_P0AF19
N-acetylglucosamine-6-phosphate deacetylase		Escherichia coli B354		397
N-acetylglucosamine-6-phosphate deacetylase		Escherichia coli O145 str. RM9872		382
N-acetylglucosamine-6-phosphate deacetylase		KLEPN		382
N-acetylglucosamine-6-phosphate deacetylase		uncultured bacterium Contig1417		382
+2326

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X14135 Genomic DNA Translation: CAA32353.1 AF052007 Genomic DNA Translation: AAC09325.1 U00096 Genomic DNA Translation: AAC73771.1 AP009048 Genomic DNA Translation: BAA35320.1
PIRⁱ	A37018
RefSeqⁱ	NP_415203.1, NC_000913.3 WP_000271153.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1YMY	X-ray	2.60	A/B	1-382	[»]
	1YRR	X-ray	2.00	A/B	1-382	[»]
	2P50	X-ray	2.20	A/B/C/D	1-382	[»]
	2P53	X-ray	2.10	A/B	1-382	[»]
ProteinModelPortalⁱ	P0AF18
SMRⁱ	P0AF18
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261208, 26 interactors
DIPⁱ	DIP-10297N
IntActⁱ	P0AF18, 5 interactors
STRINGⁱ	316385.ECDH10B_0742

Proteomic databases

EPDⁱ	P0AF18
PaxDbⁱ	P0AF18
PRIDEⁱ	P0AF18

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73771; AAC73771; b0677 BAA35320; BAA35320; BAA35320
GeneIDⁱ	945289
KEGGⁱ	ecj:JW0663 eco:b0677
PATRICⁱ	fig\|1411691.4.peg.1601

Organism-specific databases

EchoBASEⁱ	EB0626
EcoGeneⁱ	EG10632 nagA

Phylogenomic databases

eggNOGⁱ	ENOG4105CE4 Bacteria COG1820 LUCA
HOGENOMⁱ	HOG000275008
InParanoidⁱ	P0AF18
KOⁱ	K01443
OMAⁱ	HAFNAMP
PhylomeDBⁱ	P0AF18

Enzyme and pathway databases

UniPathwayⁱ	UPA00629;UER00683
BioCycⁱ	EcoCyc:NAG6PDEACET-MONOMER MetaCyc:NAG6PDEACET-MONOMER
BRENDAⁱ	3.5.1.25 2026
SABIO-RKⁱ	P0AF18

Miscellaneous databases

EvolutionaryTraceⁱ	P0AF18
Protein Ontology More...PROⁱ	PR:P0AF18

Family and domain databases

CDDⁱ	cd00854 NagA, 1 hit
Gene3Dⁱ	2.30.40.10, 2 hits
InterProⁱ	View protein in InterPro IPR006680 Amidohydro-rel IPR003764 GlcNAc_6-P_deAcase IPR011059 Metal-dep_hydrolase_composite IPR032466 Metal_Hydrolase
PANTHERⁱ	PTHR11113:SF1 PTHR11113:SF1, 1 hit
Pfamⁱ	View protein in Pfam PF01979 Amidohydro_1, 1 hit
PIRSFⁱ	PIRSF038994 NagA, 1 hit
SUPFAMⁱ	SSF51338 SSF51338, 1 hit SSF51556 SSF51556, 1 hit
TIGRFAMsⁱ	TIGR00221 nagA, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	NAGA_ECOLI
Accessionⁱ	P0AF18Primary (citable) accession number: P0AF18 Secondary accession number(s): P15300
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
	Last sequence update:	December 20, 2005
	Last modified:	October 10, 2018
	This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

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

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UniProtKB - P0AF18 (NAGA_ECOLI)

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N-acetylglucosamine-6-phosphate deacetylase

nagA

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: N-acetylneuraminate degradation

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

Pathwayⁱ: N-acetylneuraminate degradation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ