NAGA_MOUSE
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 03-AUG-2022, entry version 139.
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}.
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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 right kidney and 179 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 ACT_SITE 294
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 154..155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 232
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 235..236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 269..272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 328..330
FT /ligand="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
