ID   AGAA_ECOLI              Reviewed;         167 AA.
AC   P42906; P76670; Q2M975; Q6BF43;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 3.
DT   02-SEP-2026, entry version 149.
DE   RecName: Full=Putative N-acetylgalactosamine-6-phosphate deacetylase {ECO:0000305};
DE            Short=Aga-6-P deacetylase {ECO:0000305};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q8XAC3};
GN   Name=agaA; OrderedLocusNames=b3135, JW5527;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   SEQUENCE REVISION TO 145.
RX   PubMed=16397293; DOI=10.1093/nar/gkj405;
RA   Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA   Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA   Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA   Thomson N.R., Wishart D., Wanner B.L.;
RT   "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT   -- 2005.";
RL   Nucleic Acids Res. 34:1-9(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=8932697; DOI=10.1099/13500872-142-2-231;
RA   Reizer J., Ramseier T.M., Reizer A., Charbit A., Saier M.H. Jr.;
RT   "Novel phosphotransferase genes revealed by bacterial genome sequencing: a
RT   gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in
RT   Escherichia coli.";
RL   Microbiology 142:231-250(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-D-galactosamine 6-phosphate + H2O = D-galactosamine
CC         6-phosphate + acetate; Xref=Rhea:RHEA:18149, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:71673, ChEBI:CHEBI:71674;
CC         Evidence={ECO:0000250|UniProtKB:Q8XAC3};
CC   -!- MISCELLANEOUS: In contrast to E.coli strains C and EC3132, K-12 strains
CC       cannot grow on N-acetylgalactosamine and D-galactosamine, because they
CC       carry a deletion and thus lack active PTS systems specific for these
CC       compounds. Therefore, AgaA in K-12 strains is not involved in the
CC       degradation of these compounds.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       NagA family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57938.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U18997; AAA57938.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP009048; BAE77181.1; -; Genomic_DNA.
DR   PIR; C65103; C65103.
DR   AlphaFoldDB; P42906; -.
DR   SMR; P42906; -.
DR   BioGRID; 4261157; 5.
DR   FunCoup; P42906; 12.
DR   KEGG; ecj:JW5527; -.
DR   PATRIC; fig|83333.103.peg.4041; -.
DR   EchoBASE; EB2619; -.
DR   eggNOG; COG1820; Bacteria.
DR   HOGENOM; CLU_032482_3_1_6; -.
DR   InParanoid; P42906; -.
DR   PhylomeDB; P42906; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P42906; -.
DR   GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; ISS:UniProtKB.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR032466; Metal_Hydrolase.
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   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   5: Uncertain;
KW   Carbohydrate metabolism; Hydrolase; Reference proteome.
FT   CHAIN           1..167
FT                   /note="Putative N-acetylgalactosamine-6-phosphate
FT                   deacetylase"
FT                   /id="PRO_0000170920"
FT   CONFLICT        145
FT                   /note="S -> R (in Ref. 1; AAA57938)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   167 AA;  17519 MW;  1C3CB5AC3168FEEA CRC64;
     MHCYNGMTGL HHREPGMVGA GLTDKRAWLE LIADGHHVHP AAMSLCCCCA KERIVLITDA
     MQAAGMPDGR YTLCGEEVQM HGGVVRTASG GLAGSTLSVD AAVRNMVELT GVTPAEAIHM
     ASLHPARMLG VDGVLGSLKP GKRASVVALD SGLHVQQIWI QGQLASF
//