NAGA_DROME
ID NAGA_DROME Reviewed; 417 AA.
AC Q9VR81;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
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};
GN ORFNames=CG17065;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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 -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family. {ECO:0000305}.
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DR EMBL; AE014298; AAF50923.1; -; Genomic_DNA.
DR EMBL; AY089672; AAL90410.1; -; mRNA.
DR RefSeq; NP_001285488.1; NM_001298559.1.
DR RefSeq; NP_608380.1; NM_134536.3.
DR AlphaFoldDB; Q9VR81; -.
DR SMR; Q9VR81; -.
DR IntAct; Q9VR81; 2.
DR STRING; 7227.FBpp0290783; -.
DR PaxDb; Q9VR81; -.
DR DNASU; 33026; -.
DR EnsemblMetazoa; FBtr0077340; FBpp0077032; FBgn0031099.
DR EnsemblMetazoa; FBtr0345924; FBpp0311839; FBgn0031099.
DR GeneID; 33026; -.
DR KEGG; dme:Dmel_CG17065; -.
DR UCSC; CG17065-RA; d. melanogaster.
DR FlyBase; FBgn0031099; CG17065.
DR VEuPathDB; VectorBase:FBgn0031099; -.
DR eggNOG; KOG3892; Eukaryota.
DR HOGENOM; CLU_032482_0_2_1; -.
DR InParanoid; Q9VR81; -.
DR OrthoDB; 1066877at2759; -.
DR PhylomeDB; Q9VR81; -.
DR Reactome; R-DME-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR BioGRID-ORCS; 33026; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33026; -.
DR PRO; PR:Q9VR81; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0031099; Expressed in hemocyte (sensu Nematoda and Protostomia) and 24 other tissues.
DR ExpressionAtlas; Q9VR81; baseline and differential.
DR Genevisible; Q9VR81; DM.
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; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..417
FT /note="N-acetylglucosamine-6-phosphate deacetylase"
FT /id="PRO_0000315780"
FT ACT_SITE 305
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 155
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 166..167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 222
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 243
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 246..247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 280..283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 339..341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
SQ SEQUENCE 417 AA; 45283 MW; 99FBBFE215DE3F55 CRC64;
MDVRIKCNSE EPESPEQKIL ASSQRLLQFT NCRLVRDHRI IHDDLWVRDG RIVNPEPVFF
DERTKAHCRI DCGGAIIAPG YIDLQINGGY GVDFSYDTET IEEGVATVAR GLVKSGVTSF
CPTLVTSPSD SYHTILPRIP AEVPKGAGIL GIHAEGPFIN PQKKGAHPEH CIQTIDKGLS
TLKETYGSLE RIKIITLAPE KVTDPEVIGQ LVERGITVAL GHSMASLSDG ERAVQQGATL
ITHLFNAMLP FHHRDPGLVG LLASDAVPHG RTVYFGIISD GVHTHPAALR IAYRTHPQGL
ILVTDAISAL GLEEGVHHIG QLPLQVKQGK AFIAGTETLC GSIAPMDECV RIFQKATDCS
VVYAIEAATL HPAQCLKIEK QKGTLDFGSD ADFVLLDDQL RVLSTWIAGV CVHRTVK
