(data stored in ACNUC7421 zone)

SWISSPROT: 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   08-MAY-2019, entry version 90.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and 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
CC       of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-
CC       acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to
CC       yield glucosamine 6-phosphate and acetate. Can probably also
CC       catalyze the deacetylation of N-acetyl-D-galactosamine 6-phosphate
CC       to D-galactosamine 6-phosphate (Probable).
CC       {ECO:0000250|UniProtKB:P0AF18, 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,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57513,
CC         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;
CC       D-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
CC       function in both the N-acetyl-D-glucosamine and N-acetyl-D-
CC       galactosamine pathways. {ECO:0000269|PubMed:23634833}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. NagA family. {ECO:0000305}.
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_SDVX01000001.1.
DR   SMR; P0AF19; -.
DR   STRING; 155864.EDL933_0745; -.
DR   EnsemblBacteria; AAG54999; AAG54999; Z0824.
DR   EnsemblBacteria; BAB34130; BAB34130; BAB34130.
DR   GeneID; 917076; -.
DR   KEGG; ece:Z0824; -.
DR   KEGG; ecs:ECs0707; -.
DR   PATRIC; fig|386585.9.peg.819; -.
DR   eggNOG; ENOG4105CE4; Bacteria.
DR   eggNOG; COG1820; LUCA.
DR   HOGENOM; HOG000275008; -.
DR   KO; K01443; -.
DR   BioCyc; ECOO157:NAGA-MONOMER; -.
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:SF1; PTHR11113:SF1; 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;
DR   PRODOM; P0AF19.
DR   SWISS-2DPAGE; P0AF19.
KW   Carbohydrate metabolism; Complete proteome; Hydrolase; Metal-binding;
KW   Reference proteome.
FT   CHAIN         1    382       N-acetylglucosamine-6-phosphate
FT                                deacetylase.
FT                                /FTId=PRO_0000170916.
FT   REGION      142    143       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   REGION      219    220       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   REGION      248    251       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   REGION      306    308       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   ACT_SITE    273    273       Proton donor/acceptor.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   METAL       131    131       Divalent metal cation.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   METAL       195    195       Divalent metal cation; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   METAL       216    216       Divalent metal cation; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   BINDING     227    227       Substrate.
FT                                {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
//

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