Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N-acetylglucosamine-6-phosphate deacetylase

Gene

nagA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi63Iron 1; via tele nitrogen1 Publication1
Metal bindingi65Iron 1; via tele nitrogen1 Publication1
Metal bindingi136Iron 11 Publication1
Metal bindingi136Iron 21 Publication1
Metal bindingi202Iron 2; via tele nitrogen1 Publication1
Metal bindingi223Iron 2; via tele nitrogen1 Publication1
Binding sitei234SubstrateBy similarity1
Active sitei281Proton donor1 Publication1
Metal bindingi281Iron 11 Publication1

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processCarbohydrate metabolism
LigandIron, 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

Pathology & Biotechi

Chemistry databases

DrugBankiDB02657 Glucosamine 6-Phosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001709141 – 396N-acetylglucosamine-6-phosphate deacetylaseAdd BLAST396

Proteomic databases

PaxDbiO34450
PRIDEiO34450

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018951

Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 13Combined sources9
Beta strandi18 – 27Combined sources10
Beta strandi30 – 37Combined sources8
Beta strandi44 – 48Combined sources5
Beta strandi54 – 57Combined sources4
Beta strandi59 – 64Combined sources6
Helixi72 – 74Combined sources3
Helixi77 – 86Combined sources10
Helixi87 – 90Combined sources4
Beta strandi92 – 98Combined sources7
Helixi104 – 120Combined sources17
Helixi123 – 125Combined sources3
Beta strandi126 – 136Combined sources11
Beta strandi138 – 140Combined sources3
Helixi142 – 144Combined sources3
Helixi150 – 152Combined sources3
Helixi158 – 167Combined sources10
Turni168 – 170Combined sources3
Beta strandi172 – 177Combined sources6
Helixi179 – 181Combined sources3
Helixi183 – 185Combined sources3
Helixi186 – 193Combined sources8
Beta strandi197 – 200Combined sources4
Helixi207 – 215Combined sources9
Beta strandi220 – 223Combined sources4
Beta strandi226 – 228Combined sources3
Beta strandi233 – 235Combined sources3
Helixi237 – 244Combined sources8
Beta strandi249 – 253Combined sources5
Beta strandi255 – 259Combined sources5
Helixi261 – 271Combined sources11
Beta strandi275 – 279Combined sources5
Turni284 – 287Combined sources4
Beta strandi290 – 295Combined sources6
Beta strandi298 – 303Combined sources6
Beta strandi306 – 308Combined sources3
Helixi321 – 332Combined sources12
Helixi336 – 343Combined sources8
Helixi345 – 351Combined sources7
Turni354 – 356Combined sources3
Beta strandi357 – 359Combined sources3
Beta strandi368 – 371Combined sources4
Beta strandi377 – 382Combined sources6
Beta strandi385 – 389Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO34450

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni147 – 148Substrate binding1 Publication2
Regioni226 – 227Substrate binding1 Publication2
Regioni255 – 258Substrate binding1 Publication4
Regioni314 – 316Substrate binding1 Publication3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CE4 Bacteria
COG1820 LUCA
HOGENOMiHOG000275009
InParanoidiO34450
KOiK01443
OMAiHAFNAMP
PhylomeDBiO34450

Family and domain databases

CDDicd00854 NagA, 1 hit
Gene3Di2.30.40.10, 2 hits
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR003764 GlcNAc_6-P_deAcase
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
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
PATRICifig|224308.179.peg.3789

Entry informationi

Entry nameiNAGA_BACSU
AccessioniPrimary (citable) accession number: O34450
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 23, 2018
This is version 126 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health