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O32445 (NAGA_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
N-acetylglucosamine-6-phosphate deacetylase
EC=3.5.1.25
Alternative name(s):
GlcNAc 6-P deacetylase
Gene names
Name:nagA
Ordered Locus Names:VC_0994
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 divalent metal cation per subunit. Nickel ion is seen in the structure.

Pathway

Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the NagA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378N-acetylglucosamine-6-phosphate deacetylase
PRO_0000170918

Regions

Region216 – 2172Substrate binding
Region303 – 3053Substrate binding

Sites

Active site2701Proton donor/acceptor By similarity
Metal binding1281Divalent metal cation
Metal binding1921Divalent metal cation; via tele nitrogen
Metal binding2131Divalent metal cation; via tele nitrogen
Binding site1391Substrate; via amide nitrogen
Binding site2241Substrate
Binding site2481Substrate; via tele nitrogen

Experimental info

Sequence conflict791T → I in BAA22834. Ref.1

Secondary structure

1 ............................................................................... 378
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O32445 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 34906344A3F92A0F

FASTA37840,956
        10         20         30         40         50         60 
MYALTNCKIY TGNDVLVKHA VIINGDKIEA VCPIESLPSE MNVVDLNGAN LSPGFIDLQL 

        70         80         90        100        110        120 
NGCGGVMFND EITAETIDTM HKANLKSGCT SFLPTLITSS DENMRQAIAA AREYQAKYPN 

       130        140        150        160        170        180 
QSLGLHLEGP YLNVMKKGIH SVDFIRPSDD TMIDTICANS DVIAKVTLAP ENNKPEHIEK 

       190        200        210        220        230        240 
LVKAGIVVSI GHTNATYSEA RKSFESGITF ATHLFNAMTP MVGREPGVVG AIYDTPEVYA 

       250        260        270        280        290        300 
GIIADGFHVD YANIRIAHKI KGEKLVLVTD ATAPAGAEMD YFIFVGKKVY YRDGKCVDEN 

       310        320        330        340        350        360 
GTLGGSALTM IEAVQNTVEH VGIALDEALR MATLYPAKAI GVDEKLGRIK KGMIANLTVF 

       370 
DRDFNVKATV VNGQYEQN

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the genes for N-acetylglucosamine use that construct divergent operons (nagE-nagAC) from Vibrio cholerae non-O1."
Yamano N., Oura N., Wang J., Fujishima S.
Biosci. Biotechnol. Biochem. 61:1349-1353(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NON-O1 / 1148A.
[2]"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae."
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. expand/collapse author list , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.
Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39315 / El Tor Inaba N16961.
[3]"X-ray crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate."
Center for structural genomics of infectious diseases (CSGID)
Submitted (AUG-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEXES WITH NICKEL AND FRUCTOSE-6-PHOSPHATE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D87820 Genomic DNA. Translation: BAA22834.1.
AE003852 Genomic DNA. Translation: AAF94155.1.
PIRE82254.
JC5649.
RefSeqNP_230640.1. NC_002505.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EGJX-ray2.90A/B1-378[»]
3IV8X-ray2.53A/B/C/D1-378[»]
ProteinModelPortalO32445.
SMRO32445. Positions 1-373.
ModBaseSearch...

Protein-protein interaction databases

STRING243277.VC0994.

Protocols and materials databases

DNASU2614247.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF94155; AAF94155; VC_0994.
GeneID2614247.
KEGGvch:VC0994.
PATRIC20081086. VBIVibCho83274_0947.

Phylogenomic databases

eggNOGCOG1820.
KOK01443.
OMASGCTSYL.
ProtClustDBPRK11170.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16875.
UniPathwayUPA00629; UER00683.

Family and domain databases

InterProIPR006680. Amidohydro_1.
IPR003764. GlcNAc_6-P_deAcase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFPIRSF038994. NagA. 1 hit.
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR00221. nagA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO32445.

Entry information

Entry nameNAGA_VIBCH
AccessionPrimary (citable) accession number: O32445
Secondary accession number(s): Q9KTA9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 1, 2000
Last modified: May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant 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

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