ID NAGA_MOUSE Reviewed; 409 AA. AC Q8JZV7; Q8BK10; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 25-MAY-2022, entry version 138. DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000250|UniProtKB:Q9Y303}; DE Short=GlcNAc 6-P deacetylase {ECO:0000250|UniProtKB:Q9Y303}; DE EC=3.5.1.25 {ECO:0000250|UniProtKB:Q9Y303}; DE AltName: Full=Amidohydrolase domain-containing protein 2 {ECO:0000250|UniProtKB:Q9Y303}; GN Name=Amdhd2; 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; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Amnion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Kidney, Liver, Spleen, and Testis; 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 [4] RP PATHWAY. RX PubMed=22692205; DOI=10.1074/jbc.m112.363549; RA Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.; RT "Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating RT the intracellular fate of the non-human sialic acid N-glycolylneuraminic RT acid."; RL J. Biol. Chem. 287:28865-28881(2012). CC -!- FUNCTION: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6- CC phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) CC degradation pathway. {ECO:0000250|UniProtKB:Q9Y303}. 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:0000250|UniProtKB:Q9Y303}; 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 -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation. CC {ECO:0000269|PubMed:22692205}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC NagA family. {ECO:0000305}. 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; AK077584; BAC36877.1; -; mRNA. DR EMBL; AK090009; BAC41042.1; -; mRNA. DR EMBL; AK159860; BAE35434.1; -; mRNA. DR EMBL; AK168432; BAE40339.1; -; mRNA. DR EMBL; BC037005; AAH37005.1; -; mRNA. DR CCDS; CCDS28475.1; -. DR RefSeq; NP_766523.2; NM_172935.4. DR AlphaFoldDB; Q8JZV7; -. DR SMR; Q8JZV7; -. DR BioGRID; 232838; 1. DR STRING; 10090.ENSMUSP00000036141; -. DR MEROPS; M38.979; -. DR iPTMnet; Q8JZV7; -. DR PhosphoSitePlus; Q8JZV7; -. DR REPRODUCTION-2DPAGE; Q8JZV7; -. DR EPD; Q8JZV7; -. DR jPOST; Q8JZV7; -. DR MaxQB; Q8JZV7; -. DR PaxDb; Q8JZV7; -. DR PeptideAtlas; Q8JZV7; -. DR PRIDE; Q8JZV7; -. DR ProteomicsDB; 287603; -. DR DNASU; 245847; -. DR Ensembl; ENSMUST00000040735; ENSMUSP00000036141; ENSMUSG00000036820. DR GeneID; 245847; -. DR KEGG; mmu:245847; -. DR UCSC; uc008aum.1; mouse. DR CTD; 51005; -. DR MGI; MGI:2443978; Amdhd2. DR VEuPathDB; HostDB:ENSMUSG00000036820; -. DR eggNOG; KOG3892; Eukaryota. DR GeneTree; ENSGT00390000012605; -. DR HOGENOM; CLU_032482_0_2_1; -. DR InParanoid; Q8JZV7; -. DR OMA; HAFNAMP; -. DR OrthoDB; 1066877at2759; -. DR PhylomeDB; Q8JZV7; -. DR TreeFam; TF315036; -. DR Reactome; R-MMU-446210; Synthesis of UDP-N-acetyl-glucosamine. DR UniPathway; UPA00629; -. DR BioGRID-ORCS; 245847; 4 hits in 72 CRISPR screens. DR PRO; PR:Q8JZV7; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; Q8JZV7; protein. DR Bgee; ENSMUSG00000036820; Expressed in adult mammalian kidney and 219 other tissues. DR ExpressionAtlas; Q8JZV7; baseline and differential. DR Genevisible; Q8JZV7; MM. 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; ISS:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central. DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; TAS:UniProtKB. 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; Reference proteome. FT CHAIN 1..409 FT /note="N-acetylglucosamine-6-phosphate deacetylase" FT /id="PRO_0000315777" FT REGION 154..155 FT /note="Substrate binding" FT /evidence="ECO:0000250|UniProtKB:P0AF18" FT REGION 235..236 FT /note="Substrate binding" FT /evidence="ECO:0000250|UniProtKB:P0AF18" FT REGION 269..272 FT /note="Substrate binding" FT /evidence="ECO:0000250|UniProtKB:P0AF18" FT REGION 328..330 FT /note="Substrate binding" FT /evidence="ECO:0000250|UniProtKB:P0AF18" FT ACT_SITE 294 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P0AF18" FT METAL 143 FT /note="Divalent metal cation" FT /evidence="ECO:0000250|UniProtKB:P0AF18" FT METAL 211 FT /note="Divalent metal cation; via tele nitrogen" FT /evidence="ECO:0000250|UniProtKB:P0AF18" FT METAL 232 FT /note="Divalent metal cation; via tele nitrogen" FT /evidence="ECO:0000250|UniProtKB:P0AF18" FT BINDING 243 FT /note="Substrate" FT /evidence="ECO:0000250|UniProtKB:P0AF18" FT CONFLICT 354 FT /note="L -> M (in Ref. 1; BAC36877)" FT /evidence="ECO:0000305" SQ SEQUENCE 409 AA; 43501 MW; 914930464779CAC7 CRC64; MRSGQCAAGA PVLQFTNCRI LRGGTLLRED LWVRGGRILD PEKLFFEERR VADEQRDCGG RILAPGFIDV QINGGFGVDF SKATEDVGSG VALVARRLLS HGVTSFCPTL VTSPPEVYHK VLPQIPVKSG GPHGAGVLGV HLEGPFISRE KRGAHPEAYL RSFEANAFHD VLATYGPLDN VCIVTLAPEL DRSHEVIQAL TAQGIRVSLG HSVADLRAAE VAVQSGATFI THLFNAMLPF HHRDPGIVGL LTSDQLPPGH CIFYGMIADG IHTNPAALRI AHRAHPQGLV LVTDAVPALG LGNGRHTLGQ QEVEVDGLIA YIAGTKTLGG SIAPMDVCVR HFLQATGCSV ESALEAASLH PAQMLGLEKT KGSLDFGADA DFVVLDDTLH VQATYISGEL VWQAEEAGP //