ID F7CUP3_MOUSE Unreviewed; 446 AA. AC F7CUP3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 2. DT 13-SEP-2023, entry version 58. DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000256|ARBA:ARBA00018029}; DE EC=3.5.1.25 {ECO:0000256|ARBA:ARBA00011899}; DE AltName: Full=Amidohydrolase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00030976}; GN Name=Amdhd2 {ECO:0000313|Ensembl:ENSMUSP00000122523.3, GN ECO:0000313|MGI:MGI:2443978}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000122523.3, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000122523.3, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122523.3, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000122523.3} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122523.3}; RG Ensembl; RL Submitted (MAY-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D- CC glucosamine 6-phosphate; Xref=Rhea:RHEA:22936, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=3.5.1.25; CC Evidence={ECO:0000256|ARBA:ARBA00001570}; 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 -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation. CC {ECO:0000256|ARBA:ARBA00004878}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC NagA family. {ECO:0000256|ARBA:ARBA00010716}. 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 AlphaFoldDB; F7CUP3; -. DR SMR; F7CUP3; -. DR jPOST; F7CUP3; -. DR MaxQB; F7CUP3; -. DR PeptideAtlas; F7CUP3; -. DR ProteomicsDB; 318653; -. DR Ensembl; ENSMUST00000138685.3; ENSMUSP00000122523.3; ENSMUSG00000036820.13. DR AGR; MGI:2443978; -. DR MGI; MGI:2443978; Amdhd2. DR VEuPathDB; HostDB:ENSMUSG00000036820; -. DR GeneTree; ENSGT00390000012605; -. DR HOGENOM; CLU_2644422_0_0_1; -. DR UniPathway; UPA00629; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000036820; Expressed in right kidney and 179 other tissues. DR ExpressionAtlas; F7CUP3; baseline and differential. 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 GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd00854; NagA; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1. DR PANTHER; PTHR11113:SF14; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF038994; NagA; 2. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 2. PE 1: Evidence at protein level; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3}; KW Proteomics identification {ECO:0007829|EPD:F7CUP3, KW ECO:0007829|MaxQB:F7CUP3}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT DOMAIN 309..424 FT /note="Amidohydrolase-related" FT /evidence="ECO:0000259|Pfam:PF01979" FT ACT_SITE 338 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1" FT BINDING 187 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT BINDING 198 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT BINDING 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT BINDING 276 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT BINDING 279..280 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT BINDING 287 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT BINDING 316 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT BINDING 372..374 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" SQ SEQUENCE 446 AA; 47179 MW; B1B866E612FAA566 CRC64; MRSGQCAAGA PVLQFTNCRI LRGGTLLRED LWVRGGRILD PEKLFFEERR VADEQRDCGG RILAPGFIDV QINGGFGVDF SKATEDVGSG VALVARRLLS HGVTSFCPTL VTSPPEVYHK AHSSSYKCAR SSWALPGRPC SCEPCPHAPS PPLCFPHAAG STGKVLPQIP VKSGGPHGAG VLGVHLEGPF ISREKRGAHP EAYLRSFEAN AFHDVLATYG PLDNVCIVTL APELDRSHEV IQALTAQGIR VSLGHSVADL RAAEVAVQSG ATFITHLFNA MLPFHHRDPG IVGLLTSDQL PPGHCIFYGM IADGIHTNPA ALRIAHRAHP QGLVLVTDAV PALGLGNGRH TLGQQEVEVD GLIAYIAGTK TLGGSIAPMD VCVRHFLQAT GCSVESALEA ASLHPAQMLG LEKTKGSLDF GADAAPPPVQ ITFLDGLSFL PGLSYE //