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 06-MAR-2013, entry version 86. DE RecName: Full=Putative N-acetylglucosamine-6-phosphate deacetylase; DE EC=3.5.1.25; DE AltName: Full=Amidohydrolase domain-containing protein 2; DE AltName: Full=GlcNAc 6-P deacetylase; GN Name=Amdhd2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] 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: RT elucidating the intracellular fate of the non-human sialic acid N- RT glycolylneuraminic acid."; RL J. Biol. Chem. 287:28865-28881(2012). CC -!- FUNCTION: Hydrolyzes the N-glycolyl group from N- CC glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N- CC glycolylneuraminic acid (Neu5Gc) degradation pathway (By CC similarity). CC -!- CATALYTIC ACTIVITY: N-acetyl-D-glucosamine 6-phosphate + H(2)O = CC D-glucosamine 6-phosphate + acetate. CC -!- COFACTOR: Binds 1 divalent metal cation per subunit (By CC similarity). CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation. CC -!- SIMILARITY: Belongs to the NagA family. 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 IPI; IPI00323465; -. DR RefSeq; NP_766523.2; NM_172935.4. DR UniGene; Mm.87319; -. DR HSSP; O34450; 1UN7. DR ProteinModelPortal; Q8JZV7; -. DR SMR; Q8JZV7; 12-404. DR STRING; Q8JZV7; -. DR MEROPS; M38.979; -. DR PhosphoSite; Q8JZV7; -. DR REPRODUCTION-2DPAGE; Q8JZV7; -. DR PaxDb; Q8JZV7; -. DR PRIDE; Q8JZV7; -. 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 eggNOG; COG1820; -. DR GeneTree; ENSGT00390000012605; -. DR HOGENOM; HOG000275010; -. DR HOVERGEN; HBG108170; -. DR InParanoid; Q8JZV7; -. DR KO; K01443; -. DR OMA; DLWVREG; -. DR OrthoDB; EOG45HRXK; -. DR UniPathway; UPA00629; -. DR NextBio; 386954; -. DR Bgee; Q8JZV7; -. DR CleanEx; MM_AMDHD2; -. DR Genevestigator; Q8JZV7; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro. DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; TAS:UniProtKB. DR InterPro; IPR006680; Amidohydro_1. DR InterPro; IPR003764; GlcNAc_6-P_deAcase. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF038994; NagA; 1. DR SUPFAM; SSF51338; Metalo_hydrolase; 1. DR TIGRFAMs; TIGR00221; nagA; 1. PE 2: Evidence at transcript level; KW Carbohydrate metabolism; Complete proteome; Hydrolase; Metal-binding; KW Reference proteome. FT CHAIN 1 409 Putative N-acetylglucosamine-6-phosphate FT deacetylase. FT /FTId=PRO_0000315777. FT REGION 235 236 Substrate binding (By similarity). FT REGION 328 330 Substrate binding (By similarity). FT ACT_SITE 294 294 Proton donor/acceptor (By similarity). FT METAL 143 143 Divalent metal cation (By similarity). FT METAL 211 211 Divalent metal cation; via tele nitrogen FT (By similarity). FT METAL 232 232 Divalent metal cation; via tele nitrogen FT (By similarity). FT BINDING 154 154 Substrate; via amide nitrogen (By FT similarity). FT BINDING 243 243 Substrate (By similarity). FT BINDING 272 272 Substrate; via tele nitrogen (By FT similarity). FT CONFLICT 354 354 L -> M (in Ref. 1; BAC36877). 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 //