ID   NAGA_ECO57              Reviewed;         382 AA.
AC   P0AF19; P15300;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   02-SEP-2026, entry version 117.
DE   RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000250|UniProtKB:P0AF18};
DE            Short=GlcNAc 6-P deacetylase {ECO:0000250|UniProtKB:P0AF18};
DE            EC=3.5.1.25 {ECO:0000250|UniProtKB:P0AF18};
GN   Name=nagA; OrderedLocusNames=Z0824, ECs0707;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=23634833; DOI=10.1186/1471-2180-13-94;
RA   Hu Z., Patel I.R., Mukherjee A.;
RT   "Genetic analysis of the roles of agaA, agaI, and agaS genes in the N-
RT   acetyl-D-galactosamine and D-galactosamine catabolic pathways in
RT   Escherichia coli strains O157:H7 and C.";
RL   BMC Microbiol. 13:94-94(2013).
CC   -!- FUNCTION: Involved in the first committed step in the biosynthesis of
CC       amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group
CC       of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-
CC       phosphate and acetate. Can probably also catalyze the deacetylation of
CC       N-acetyl-D-galactosamine 6-phosphate to D-galactosamine 6-phosphate
CC       (Probable). {ECO:0000250|UniProtKB:P0AF18,
CC       ECO:0000305|PubMed:23634833}.
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:P0AF18};
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   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC       fructose 6-phosphate from N-acetylneuraminate: step 4/5.
CC       {ECO:0000250|UniProtKB:P0AF18}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AF18}.
CC   -!- INDUCTION: Induced by growth on N-acetyl-D-glucosamine but not by
CC       growth on N-acetyl-D-galactosamine. {ECO:0000269|PubMed:23634833}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant can grow on N-acetyl-D-
CC       galactosamine but not on N-acetyl-D-glucosamine.
CC       {ECO:0000269|PubMed:23634833}.
CC   -!- MISCELLANEOUS: NagA and AgaA can substitute for each other and function
CC       in both the N-acetyl-D-glucosamine and N-acetyl-D-galactosamine
CC       pathways. {ECO:0000269|PubMed:23634833}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       NagA family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG54999.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34130.1; -; Genomic_DNA.
DR   PIR; C85567; C85567.
DR   PIR; C90717; C90717.
DR   RefSeq; NP_308734.1; NC_002695.2.
DR   RefSeq; WP_000271153.1; NZ_AP018488.1.
DR   AlphaFoldDB; P0AF19; -.
DR   SMR; P0AF19; -.
DR   STRING; 155864.Z0824; -.
DR   GeneID; 75170675; -.
DR   GeneID; 75204968; -.
DR   GeneID; 917076; -.
DR   KEGG; ece:Z0824; -.
DR   KEGG; ecs:ECs_0707; -.
DR   PATRIC; fig|386585.9.peg.819; -.
DR   eggNOG; COG1820; Bacteria.
DR   HOGENOM; CLU_032482_2_2_6; -.
DR   OMA; PCRKGAH; -.
DR   UniPathway; UPA00629; UER00683.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0006046; P:N-acetylglucosamine catabolic process; ISS:UniProtKB.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   CDD; cd00854; NagA; 1.
DR   FunFam; 3.20.20.140:FF:000004; 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   NCBIfam; NF008371; PRK11170.1; 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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..382
FT                   /note="N-acetylglucosamine-6-phosphate deacetylase"
FT                   /id="PRO_0000170916"
FT   ACT_SITE        273
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         131
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         142..143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         195
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         216
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         219..220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         248..251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
FT   BINDING         306..308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AF18"
SQ   SEQUENCE   382 AA;  40949 MW;  A10B015ADFC98FCA CRC64;
     MYALTQGRIF TGHEFLDDHA VVIADGLIKS VCPVAELPPE IEQRSLNGAI LSPGFIDVQL
     NGCGGVQFND TAEAVSVETL EIMQKANEKS GCTNYLPTLI TTSDELMKQG VRVMREYLAK
     HPNQALGLHL EGPWLNLVKK GTHNPNFVRK PDAALVDFLC ENADVITKVT LAPEMVPAEV
     ISKLANAGIV VSAGHSNATL KEAKAGFRAG ITFATHLYNA MPYITGREPG LAGAILDEAD
     IYCGIIADGL HVDYANIRNA KRLKGDKLCL VTDATAPAGA NIEQFIFAGK TIYYRNGLCV
     DENGTLSGSS LTMIEGVRNL VEHCGIALDE VLRMATLYPA RAIGVEKRLG TLAAGKVANL
     TAFTPDFKIT KTIVNGNEVV TQ
//