NAGA_ECO57
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 03-AUG-2022, entry version 101.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=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: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_002695.1.
DR RefSeq; WP_000271153.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AF19; -.
DR SMR; P0AF19; -.
DR STRING; 155864.EDL933_0745; -.
DR EnsemblBacteria; AAG54999; AAG54999; Z0824.
DR EnsemblBacteria; BAB34130; BAB34130; ECs_0707.
DR GeneID; 66671053; -.
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; HAFNAMP; -.
DR UniPathway; UPA00629; UER00683.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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 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 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
