(data stored in ACNUC7421 zone)

SWISSPROT: B7UKU9_ECO27

ID   B7UKU9_ECO27            Unreviewed;       382 AA.
AC   B7UKU9;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:CAS08107.1};
GN   Name=nagA {ECO:0000313|EMBL:CAS08107.1};
GN   OrderedLocusNames=E2348C_0559 {ECO:0000313|EMBL:CAS08107.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08107.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08107.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038994-3};
CC       Note=Binds 1 divalent metal cation per subunit.
CC       {ECO:0000256|PIRSR:PIRSR038994-3};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. NagA family. {ECO:0000256|PIRNR:PIRNR038994}.
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DR   EMBL; FM180568; CAS08107.1; -; Genomic_DNA.
DR   RefSeq; WP_000271154.1; NC_011601.1.
DR   SMR; B7UKU9; -.
DR   EnsemblBacteria; CAS08107; CAS08107; E2348C_0559.
DR   KEGG; ecg:E2348C_0559; -.
DR   HOGENOM; HOG000275008; -.
DR   KO; K01443; -.
DR   OMA; HAFNAMP; -.
DR   BioCyc; ECOL574521:E2348C_RS02965-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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   3: Inferred from homology;
DR   PRODOM; B7UKU9.
DR   SWISS-2DPAGE; B7UKU9.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR038994};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR038994};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3}.
FT   DOMAIN       50    379       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   REGION      219    220       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR038994-2}.
FT   REGION      306    308       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR038994-2}.
FT   ACT_SITE    273    273       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR038994-1}.
FT   METAL       131    131       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR038994-3}.
FT   METAL       195    195       Divalent metal cation; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-3}.
FT   METAL       216    216       Divalent metal cation; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-3}.
FT   BINDING     142    142       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-2}.
FT   BINDING     227    227       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR038994-2}.
FT   BINDING     251    251       Substrate; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-2}.
SQ   SEQUENCE   382 AA;  40977 MW;  A10B0145E2C98FCA 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 RTIVNGNEVV TQ
//

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