NAGA_CAEEL
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 03-AUG-2022, entry version 140.
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=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-
CC glucosamine 6-phosphate; 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_498990.1; NM_066589.5.
DR AlphaFoldDB; P34480; -.
DR SMR; P34480; -.
DR BioGRID; 41471; 2.
DR DIP; DIP-24730N; -.
DR IntAct; P34480; 1.
DR STRING; 6239.F59B2.3.2; -.
DR EPD; P34480; -.
DR PaxDb; P34480; -.
DR PeptideAtlas; P34480; -.
DR EnsemblMetazoa; F59B2.3.1; F59B2.3.1; WBGene00010308.
DR UCSC; F59B2.3.2; c. elegans.
DR WormBase; F59B2.3; CE00231; WBGene00010308; -.
DR eggNOG; KOG3892; Eukaryota.
DR GeneTree; ENSGT00390000012605; -.
DR HOGENOM; CLU_032482_0_2_1; -.
DR InParanoid; P34480; -.
DR OMA; HAFNAMP; -.
DR OrthoDB; 1066877at2759; -.
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 tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR CDD; cd00854; NagA; 1.
DR Gene3D; 2.30.40.10; -; 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 PANTHER; PTHR11113:SF14; PTHR11113:SF14; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF038994; NagA; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR00221; nagA; 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
