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Protein

N-acetylglucosamine-6-phosphate deacetylase

Gene

nagA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the first committed 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.1 Publication

Catalytic activityi

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

Cofactori

a divalent metal cation1 PublicationNote: Binds 2 divalent metal cations per subunit.1 Publication

Pathwayi: N-acetylneuraminate degradation

This protein is involved in step 4 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.Curated
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. N-acetylglucosamine-6-phosphate deacetylase (nagA)
  5. Glucosamine-6-phosphate deaminase 1 (nagB), Probable glucosamine-6-phosphate deaminase 2 (gamA)
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Iron 1; via tele nitrogen1 Publication
Metal bindingi65 – 651Iron 1; via tele nitrogen1 Publication
Metal bindingi136 – 1361Iron 11 Publication
Metal bindingi136 – 1361Iron 21 Publication
Metal bindingi202 – 2021Iron 2; via tele nitrogen1 Publication
Metal bindingi223 – 2231Iron 2; via tele nitrogen1 Publication
Binding sitei234 – 2341SubstrateBy similarity
Active sitei281 – 2811Proton donor1 Publication
Metal bindingi281 – 2811Iron 11 Publication

GO - Molecular functioni

  • iron ion binding Source: UniProtKB
  • N-acetylglucosamine-6-phosphate deacetylase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU35010-MONOMER.
SABIO-RKO34450.
UniPathwayiUPA00629; UER00683.

Protein family/group databases

MEROPSiM38.983.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylglucosamine-6-phosphate deacetylase1 Publication (EC:3.5.1.25By similarity)
Short name:
GlcNAc 6-P deacetylase1 Publication
Gene namesi
Name:nagA
Ordered Locus Names:BSU35010
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396N-acetylglucosamine-6-phosphate deacetylasePRO_0000170914Add
BLAST

Proteomic databases

PaxDbiO34450.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018951.

Structurei

Secondary structure

1
396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Beta strandi18 – 2710Combined sources
Beta strandi30 – 378Combined sources
Beta strandi44 – 485Combined sources
Beta strandi54 – 574Combined sources
Beta strandi59 – 646Combined sources
Helixi72 – 743Combined sources
Helixi77 – 8610Combined sources
Helixi87 – 904Combined sources
Beta strandi92 – 987Combined sources
Helixi104 – 12017Combined sources
Helixi123 – 1253Combined sources
Beta strandi126 – 13611Combined sources
Beta strandi138 – 1403Combined sources
Helixi142 – 1443Combined sources
Helixi150 – 1523Combined sources
Helixi158 – 16710Combined sources
Turni168 – 1703Combined sources
Beta strandi172 – 1776Combined sources
Helixi179 – 1813Combined sources
Helixi183 – 1853Combined sources
Helixi186 – 1938Combined sources
Beta strandi197 – 2004Combined sources
Helixi207 – 2159Combined sources
Beta strandi220 – 2234Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi233 – 2353Combined sources
Helixi237 – 2448Combined sources
Beta strandi249 – 2535Combined sources
Beta strandi255 – 2595Combined sources
Helixi261 – 27111Combined sources
Beta strandi275 – 2795Combined sources
Turni284 – 2874Combined sources
Beta strandi290 – 2956Combined sources
Beta strandi298 – 3036Combined sources
Beta strandi306 – 3083Combined sources
Helixi321 – 33212Combined sources
Helixi336 – 3438Combined sources
Helixi345 – 3517Combined sources
Turni354 – 3563Combined sources
Beta strandi357 – 3593Combined sources
Beta strandi368 – 3714Combined sources
Beta strandi377 – 3826Combined sources
Beta strandi385 – 3895Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VHLX-ray2.05A/B1-396[»]
ProteinModelPortaliO34450.
SMRiO34450. Positions 2-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34450.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 1482Substrate binding1 Publication
Regioni226 – 2272Substrate binding1 Publication
Regioni255 – 2584Substrate binding1 Publication
Regioni314 – 3163Substrate binding1 Publication

Sequence similaritiesi

Belongs to the NagA family.Curated

Phylogenomic databases

eggNOGiENOG4105CE4. Bacteria.
COG1820. LUCA.
HOGENOMiHOG000275009.
InParanoidiO34450.
KOiK01443.
OMAiAFITDAM.
PhylomeDBiO34450.

Family and domain databases

CDDicd00854. NagA. 1 hit.
Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR003764. GlcNAc_6-P_deAcase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFiPIRSF038994. NagA. 1 hit.
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR00221. nagA. 1 hit.

Sequencei

Sequence statusi: Complete.

O34450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAESLLIKDI AIVTENEVIK NGYVGINDGK ISTVSTERPK EPYSKEIQAP
60 70 80 90 100
ADSVLLPGMI DIHIHGGYGA DTMDASFSTL DIMSSRLPEE GTTSFLATTI
110 120 130 140 150
TQEHGNISQA LVNAREWKAA EESSLLGAEL LGIHLEGPFV SPKRAGAQPK
160 170 180 190 200
EWIRPSDVEL FKKWQQEAGG LIKIVTLAPE EDQHFELIRH LKDESIIASM
210 220 230 240 250
GHTDADSALL SDAAKAGASH MTHLYNAMSP FHHREPGVIG TALAHDGFVT
260 270 280 290 300
ELIADGIHSH PLAAKLAFLA KGSSKLILIT DSMRAKGLKD GVYEFGGQSV
310 320 330 340 350
TVRGRTALLS DGTLAGSILK MNEGARHMRE FTNCSWTDIA NITSENAAKQ
360 370 380 390
LGIFDRKGSV TVGKDADLVI VSSDCEVILT ICRGNIAFIS KEADQI
Length:396
Mass (Da):42,622
Last modified:January 1, 1998 - v1
Checksum:i852D53C71BAD6F54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017113 Genomic DNA. Translation: AAC67285.1.
AL009126 Genomic DNA. Translation: CAB15506.1.
PIRiA69664.
RefSeqiNP_391381.1. NC_000964.3.
WP_003243413.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15506; CAB15506; BSU35010.
GeneIDi936621.
KEGGibsu:BSU35010.
PATRICi18979008. VBIBacSub10457_3666.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017113 Genomic DNA. Translation: AAC67285.1.
AL009126 Genomic DNA. Translation: CAB15506.1.
PIRiA69664.
RefSeqiNP_391381.1. NC_000964.3.
WP_003243413.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VHLX-ray2.05A/B1-396[»]
ProteinModelPortaliO34450.
SMRiO34450. Positions 2-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018951.

Protein family/group databases

MEROPSiM38.983.

Proteomic databases

PaxDbiO34450.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15506; CAB15506; BSU35010.
GeneIDi936621.
KEGGibsu:BSU35010.
PATRICi18979008. VBIBacSub10457_3666.

Phylogenomic databases

eggNOGiENOG4105CE4. Bacteria.
COG1820. LUCA.
HOGENOMiHOG000275009.
InParanoidiO34450.
KOiK01443.
OMAiAFITDAM.
PhylomeDBiO34450.

Enzyme and pathway databases

UniPathwayiUPA00629; UER00683.
BioCyciBSUB:BSU35010-MONOMER.
SABIO-RKO34450.

Miscellaneous databases

EvolutionaryTraceiO34450.

Family and domain databases

CDDicd00854. NagA. 1 hit.
Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR003764. GlcNAc_6-P_deAcase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFiPIRSF038994. NagA. 1 hit.
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR00221. nagA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNAGA_BACSU
AccessioniPrimary (citable) accession number: O34450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.