AGAA_ECO57
ID AGAA_ECO57 Reviewed; 377 AA.
AC Q8XAC3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=N-acetylgalactosamine-6-phosphate deacetylase {ECO:0000305};
DE Short=Aga-6-P deacetylase {ECO:0000303|PubMed:23634833};
DE EC=3.5.1.- {ECO:0000305|PubMed:23634833};
GN Name=agaA; OrderedLocusNames=Z4489 {ECO:0000312|EMBL:AAG58267.1};
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 FUNCTION, CATALYTIC ACTIVITY, 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: Catalyzes the deacetylation of N-acetyl-D-galactosamine 6-
CC phosphate to D-galactosamine 6-phosphate. Can probably also catalyze
CC the deacetylation of N-acetyl-D-glucosamine 6-phosphate to D-
CC glucosamine 6-phosphate. {ECO:0000305|PubMed:23634833}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-galactosamine 6-phosphate = acetate + D-
CC galactosamine 6-phosphate; Xref=Rhea:RHEA:18149, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:71673, ChEBI:CHEBI:71674;
CC Evidence={ECO:0000305|PubMed:23634833};
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 -!- INDUCTION: Induced by growth on N-acetyl-D-galactosamine but not by
CC growth on N-acetyl-D-glucosamine. {ECO:0000269|PubMed:23634833}.
CC -!- DISRUPTION PHENOTYPE: AgaA deletion mutant, but not agaA-nagA double
CC mutant, can grow on N-acetyl-D-galactosamine. AgaA deletion mutant is
CC probably able to grow on N-acetyl-D-galactosamine because NagA can
CC substitute for the absence of AgaA. Deletion of agaA does not affect N-
CC acetyl-D-glucosamine utilization. {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; AAG58267.1; -; Genomic_DNA.
DR PIR; G85975; G85975.
DR PIR; G91130; G91130.
DR RefSeq; WP_001301829.1; NZ_SEKU01000004.1.
DR AlphaFoldDB; Q8XAC3; -.
DR SMR; Q8XAC3; -.
DR STRING; 155864.EDL933_4357; -.
DR EnsemblBacteria; AAG58267; AAG58267; Z4489.
DR KEGG; ece:Z4489; -.
DR PATRIC; fig|83334.175.peg.701; -.
DR eggNOG; COG1820; Bacteria.
DR OMA; YMKNPRL; -.
DR BioCyc; MetaCyc:MON-18273; -.
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:RHEA.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Hydrolase; Metal-binding.
FT CHAIN 1..377
FT /note="N-acetylgalactosamine-6-phosphate deacetylase"
FT /id="PRO_0000441910"
FT ACT_SITE 269
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 125
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 136..137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 191
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 212
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 215..216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 244..247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 302..304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
SQ SEQUENCE 377 AA; 40270 MW; DC04BB23976C3CEC CRC64;
MTHVLRARRL LTEEGWLDDH QLRIADGVIA AIEPIPVSVT ERDAELLCPA YIDTHVHGGA
GVDVMDDAPD VLDKLAMHKA REGVGSWLPT TVTAPLSTIH AALKRIAQRC QRGGPGAQVL
GSYLEGPYFT PQNKGAHPPE LFRELEIAEL DQLIAVSQHT LRVVALAPEK EGALQAIRHL
KQQNVRVMLG HSAATWQQTR AAFDAGADGL VHCYNGMTGL HHREPGMVGA GLTDKRAWLE
LIADGHHVHP AAMSLCCCCA KERIVLITDA MQAAGMPDGR YTLCGEEVQM HGGVVRTASG
GLAGSTLSVD AAVRNMVELT GVTPAEAIHM ASLHPARMLG VDGVLGSLKP GKRASVVALD
SGLHVQQIWI QGQLASF
