ID A0A6I4RZS3_FRATU Unreviewed; 377 AA. AC A0A6I4RZS3; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 14-DEC-2022, entry version 8. DE SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:MWZ50658.1}; DE EC=3.5.1.25 {ECO:0000313|EMBL:MWZ50658.1}; GN Name=nagA {ECO:0000313|EMBL:MWZ50658.1}; GN ORFNames=FNC42_02205 {ECO:0000313|EMBL:MWZ50658.1}; OS Francisella tularensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=263 {ECO:0000313|EMBL:MWZ50658.1, ECO:0000313|Proteomes:UP000460339}; RN [1] {ECO:0000313|EMBL:MWZ50658.1, ECO:0000313|Proteomes:UP000460339} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=08-1280 {ECO:0000313|EMBL:MWZ50658.1, RC ECO:0000313|Proteomes:UP000460339}; RA Kevin M., Madani N., Maurin M.; RT "Phylogeography and genetic diversity of Francisella tularensis subsp. RT holarctica in France (1947-2018)."; RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases. 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 superfamily. CC NagA family. {ECO:0000256|ARBA:ARBA00010716, CC ECO:0000256|PIRNR:PIRNR038994}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MWZ50658.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VJFB01000005; MWZ50658.1; -; Genomic_DNA. DR RefSeq; WP_003026430.1; NZ_VJFB01000005.1. DR AlphaFoldDB; A0A6I4RZS3; -. DR Proteomes; UP000460339; Unassembled WGS sequence. 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; IEA:UniProtKB-EC. 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; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF038994; NagA; 1. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR TIGRFAMs; TIGR00221; nagA; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|PIRNR:PIRNR038994}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR038994, ECO:0000313|EMBL:MWZ50658.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3}. FT DOMAIN 53..375 FT /note="Amidohydro-rel" FT /evidence="ECO:0000259|Pfam:PF01979" FT ACT_SITE 278 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1" FT BINDING 133 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT BINDING 199 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" SQ SEQUENCE 377 AA; 40582 MW; 86EAB0DDB1B9D270 CRC64; MQSYILKGGK IYSQNDFEAK DIVVKDNVIS DIVDDADPAA FNLPIIELSG DDYVIPGFID IHIHGSKGAD VMDGDVDALA VISKSLYTQG VTSYLATTMT AANEQILKAM RAIKDYNSQT HLDSAKIVGV HLEGPFISPG KIGAQNPNYL QEADVTKMAS WHNACDSLIK KITIAPEIKN ANKVIEFCNS KNIISSIGHT SCTMAQALNA IEQGCTHATH LFNAMSPIEH RNPGAATALL MSKKVLAELI VDGIHLHPDM VKFTYAIKGS DKIALITDAM SAQSAGEGVF ELGGQKVIVK DGQARLENGV FAGSVLTMNK ALENVLKFTN CSLYDAVKMT STNQAKSLGF KKGQIKGGFD AEFVILNKNY QVKQVIG //