ID   NAGA_CAEEL              Reviewed;         418 AA.
AC   P34480;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 158.
DE   RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000250|UniProtKB:Q9Y303};
DE            Short=GlcNAc 6-P deacetylase {ECO:0000250|UniProtKB:Q9Y303};
DE            EC=3.5.1.25 {ECO:0000250|UniProtKB:Q9Y303};
GN   ORFNames=F59B2.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-
CC         phosphate + acetate; Xref=Rhea:RHEA:22936, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=3.5.1.25;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y303};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P0AF18};
CC       Note=Binds 1 divalent metal cation per subunit.
CC       {ECO:0000250|UniProtKB:P0AF18};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       NagA family. {ECO:0000305}.
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DR   EMBL; Z11505; CAA77585.1; -; Genomic_DNA.
DR   PIR; S31124; S31124.
DR   RefSeq; NP_001366671.1; NM_001379854.2.
DR   AlphaFoldDB; P34480; -.
DR   SMR; P34480; -.
DR   BioGRID; 41471; 3.
DR   DIP; DIP-24730N; -.
DR   FunCoup; P34480; 795.
DR   IntAct; P34480; 1.
DR   STRING; 6239.F59B2.3.3; -.
DR   PaxDb; 6239-F59B2.3.3; -.
DR   PeptideAtlas; P34480; -.
DR   EnsemblMetazoa; F59B2.3.1; F59B2.3.1; WBGene00010308.
DR   GeneID; 176272; -.
DR   KEGG; cel:CELE_F59B2.3; -.
DR   UCSC; F59B2.3.2; c. elegans.
DR   AGR; WB:WBGene00010308; -.
DR   CTD; 176272; -.
DR   WormBase; F59B2.3; CE00231; WBGene00010308; -.
DR   eggNOG; KOG3892; Eukaryota.
DR   HOGENOM; CLU_032482_0_2_1; -.
DR   InParanoid; P34480; -.
DR   OMA; PCRKGAH; -.
DR   OrthoDB; 10264777at2759; -.
DR   PhylomeDB; P34480; -.
DR   Reactome; R-CEL-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR   PRO; PR:P34480; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00010308; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0106279; P:negative regulation of UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-ARBA.
DR   CDD; cd00854; NagA; 1.
DR   FunFam; 3.20.20.140:FF:000023; N-acetylglucosamine-6-phosphate deacetylase; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR003764; GlcNAc_6-P_deAcase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR00221; nagA; 1.
DR   PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR   PANTHER; PTHR11113:SF14; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF038994; NagA; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..418
FT                   /note="N-acetylglucosamine-6-phosphate deacetylase"
FT                   /id="PRO_0000170912"
FT   ACT_SITE        306
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         154
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         165..166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         223
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         244
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         247..248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         281..284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         340..342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
SQ   SEQUENCE   418 AA;  44887 MW;  4988EA416F5D1247 CRC64;
     MLPRKLKIDS TELAEITNEL VQFLNCLVLR SGGLKKEHIW VRNGRILDER TVFFEEKTMA
     DVQIDCEGLI LSPGFIDLQL NGGFGIDFST YNSDDKEYQE GLALVAKQLL AHGVTSFSPT
     VITSSPETYH KILPLLKPSN ASSEGAGNLG AHLEGPFISA DKRGCHPEQL VITSLSPNPV
     EIIEHVYGST ENIAIVTMAP ELEGAQEAIE YFVSTGTTVS VGHSSAKLGP GEMAVLSGAK
     MITHLFNAMQ SYHHRDPGLI GLLTSSKLTP DHPLYYGIIS DGIHTHDSAL RIAYHTNSAG
     LVLVTDAIAA LGMSDGVHKL GTQTIHVKGL EAKLDGTNTT AGSVASMPYC IRHLMKATGC
     PIEFALQSAT HKPATLLGVS DEKGTLDVGR LADFVLIDKN VTVKATFCSG KRVFLAQD
//