NAGK_ARATH
ID NAGK_ARATH Reviewed; 347 AA.
AC Q9SCL7; Q8LA25;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Acetylglutamate kinase, chloroplastic {ECO:0000305};
DE EC=2.7.2.8 {ECO:0000269|PubMed:16377628};
DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000305};
DE AltName: Full=NAG kinase {ECO:0000303|PubMed:16377628};
DE Short=AtNAGK {ECO:0000303|PubMed:16377628};
DE Flags: Precursor;
GN Name=NAGK {ECO:0000303|PubMed:16377628};
GN OrderedLocusNames=At3g57560 {ECO:0000312|Araport:AT3G57560};
GN ORFNames=T8H10.160 {ECO:0000312|EMBL:CAB66113.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=16545809; DOI=10.1016/j.febslet.2006.02.075;
RA Ferrario-Mery S., Besin E., Pichon O., Meyer C., Hodges M.;
RT "The regulatory PII protein controls arginine biosynthesis in
RT Arabidopsis.";
RL FEBS Lett. 580:2015-2020(2006).
RN [6]
RP PROTEIN SEQUENCE OF 51-58, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GLB1,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16377628; DOI=10.1074/jbc.m510945200;
RA Chen Y.M., Ferrar T.S., Lohmeier-Vogel E.M., Lohmeir-Vogel E., Morrice N.,
RA Mizuno Y., Berenger B., Ng K.K., Muench D.G., Moorhead G.B.;
RT "The PII signal transduction protein of Arabidopsis thaliana forms an
RT arginine-regulated complex with plastid N-acetyl glutamate kinase.";
RL J. Biol. Chem. 281:5726-5733(2006).
RN [7]
RP ACTIVITY REGULATION, AND INTERACTION WITH GLB1.
RX PubMed=19631611; DOI=10.1016/j.bbrc.2009.07.088;
RA Feria Bourrellier A.B., Ferrario-Mery S., Vidal J., Hodges M.;
RT "Metabolite regulation of the interaction between Arabidopsis thaliana PII
RT and N-acetyl-l-glutamate kinase.";
RL Biochem. Biophys. Res. Commun. 387:700-704(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-51, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 51-347 IN COMPLEX WITH
RP N-ACETYL-L-GLUTAMATE; L-ARGININE; ATP AND ADP, AND INTERACTION WITH GLB1.
RX PubMed=17913711; DOI=10.1074/jbc.m707127200;
RA Mizuno Y., Moorhead G.B., Ng K.K.;
RT "Structural basis for the regulation of N-acetylglutamate kinase by PII in
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 282:35733-35740(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 51-347 IN COMPLEX WITH ADP;
RP L-ARGININE AND N-ACETYL-L-GLUTAMATE.
RX PubMed=25416954; DOI=10.1016/j.cell.2014.10.015;
RA Chellamuthu V.R., Ermilova E., Lapina T., Luddecke J., Minaeva E.,
RA Herrmann C., Hartmann M.D., Forchhammer K.;
RT "A widespread glutamine-sensing mechanism in the plant kingdom.";
RL Cell 159:1188-1199(2014).
CC -!- FUNCTION: Involved in the arginine biosynthetic pathway via the
CC intermediate compound ornithine. {ECO:0000269|PubMed:16377628,
CC ECO:0000269|PubMed:16545809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-
CC phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8;
CC Evidence={ECO:0000269|PubMed:16377628};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14630;
CC Evidence={ECO:0000269|PubMed:16377628};
CC -!- ACTIVITY REGULATION: Inhibited by arginine. Inhibition is relieved by
CC binding to GLB1. {ECO:0000269|PubMed:16377628,
CC ECO:0000269|PubMed:19631611}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.08 mM for N-acetyl glutamate (NAG)
CC {ECO:0000269|PubMed:16377628};
CC Vmax=10.6 mmol/min/mg enzyme with N-acetyl glutamate (NAG) as
CC substrate {ECO:0000269|PubMed:16377628};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4. {ECO:0000305|PubMed:17913711}.
CC -!- SUBUNIT: Interacts with GLB1. Interaction is dependent of MgATP and
CC inhibited by 2-oxoglutarate, arginine, glutamate, citrate, and
CC oxaloacetate. {ECO:0000269|PubMed:16377628,
CC ECO:0000269|PubMed:17913711, ECO:0000269|PubMed:19631611}.
CC -!- INTERACTION:
CC Q9SCL7; Q9ZST4: GLB1; NbExp=5; IntAct=EBI-701276, EBI-701245;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:16377628}.
CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC subfamily. {ECO:0000305}.
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DR EMBL; AL133248; CAB66113.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79672.1; -; Genomic_DNA.
DR EMBL; AY035107; AAK59612.1; -; mRNA.
DR EMBL; AY113901; AAM44949.1; -; mRNA.
DR EMBL; AY088067; AAM65613.1; -; mRNA.
DR PIR; T46192; T46192.
DR RefSeq; NP_191315.1; NM_115616.3.
DR PDB; 2RD5; X-ray; 2.51 A; A/B=51-347.
DR PDB; 4USJ; X-ray; 2.85 A; A/B=51-347.
DR PDBsum; 2RD5; -.
DR PDBsum; 4USJ; -.
DR AlphaFoldDB; Q9SCL7; -.
DR SMR; Q9SCL7; -.
DR BioGRID; 10239; 3.
DR DIP; DIP-53401N; -.
DR IntAct; Q9SCL7; 3.
DR STRING; 3702.AT3G57560.1; -.
DR iPTMnet; Q9SCL7; -.
DR MetOSite; Q9SCL7; -.
DR PaxDb; Q9SCL7; -.
DR PRIDE; Q9SCL7; -.
DR ProteomicsDB; 251271; -.
DR EnsemblPlants; AT3G57560.1; AT3G57560.1; AT3G57560.
DR GeneID; 824923; -.
DR Gramene; AT3G57560.1; AT3G57560.1; AT3G57560.
DR KEGG; ath:AT3G57560; -.
DR Araport; AT3G57560; -.
DR TAIR; locus:2103528; AT3G57560.
DR eggNOG; KOG2436; Eukaryota.
DR HOGENOM; CLU_053680_0_1_1; -.
DR InParanoid; Q9SCL7; -.
DR OMA; EGLYEDW; -.
DR OrthoDB; 1290833at2759; -.
DR PhylomeDB; Q9SCL7; -.
DR BioCyc; ARA:AT3G57560-MON; -.
DR BRENDA; 2.7.2.8; 399.
DR SABIO-RK; Q9SCL7; -.
DR UniPathway; UPA00068; UER00107.
DR EvolutionaryTrace; Q9SCL7; -.
DR PRO; PR:Q9SCL7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCL7; baseline and differential.
DR Genevisible; Q9SCL7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IDA:TAIR.
DR GO; GO:0034618; F:arginine binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; TAS:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04250; AAK_NAGK-C; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR HAMAP; MF_00082; ArgB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR037528; ArgB.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR041727; NAGK-C.
DR Pfam; PF00696; AA_kinase; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR00761; argB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis; Arginine biosynthesis;
KW ATP-binding; Chloroplast; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:16377628,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 51..347
FT /note="Acetylglutamate kinase, chloroplastic"
FT /id="PRO_0000401370"
FT BINDING 94..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25416954,
FT ECO:0007744|PDB:4USJ"
FT BINDING 126
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /evidence="ECO:0000269|PubMed:25416954,
FT ECO:0007744|PDB:4USJ"
FT BINDING 148
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /evidence="ECO:0000269|PubMed:17913711,
FT ECO:0000269|PubMed:25416954, ECO:0007744|PDB:2RD5,
FT ECO:0007744|PDB:4USJ"
FT BINDING 242..245
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /evidence="ECO:0000269|PubMed:17913711,
FT ECO:0000269|PubMed:25416954, ECO:0007744|PDB:2RD5,
FT ECO:0007744|PDB:4USJ"
FT BINDING 260
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:17913711,
FT ECO:0000269|PubMed:25416954, ECO:0007744|PDB:2RD5,
FT ECO:0007744|PDB:4USJ"
FT BINDING 265..266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25416954,
FT ECO:0007744|PDB:4USJ"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17913711,
FT ECO:0000269|PubMed:25416954, ECO:0007744|PDB:2RD5,
FT ECO:0007744|PDB:4USJ"
FT BINDING 282
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:17913711,
FT ECO:0000269|PubMed:25416954, ECO:0007744|PDB:2RD5,
FT ECO:0007744|PDB:4USJ"
FT BINDING 297..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17913711,
FT ECO:0007744|PDB:2RD5"
FT BINDING 334..337
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:17913711,
FT ECO:0000269|PubMed:25416954, ECO:0007744|PDB:2RD5,
FT ECO:0007744|PDB:4USJ"
FT BINDING 342
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:17913711,
FT ECO:0000269|PubMed:25416954, ECO:0007744|PDB:2RD5,
FT ECO:0007744|PDB:4USJ"
FT MOD_RES 51
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:2RD5"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 259..275
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:2RD5"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2RD5"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:2RD5"
SQ SEQUENCE 347 AA; 36595 MW; 96F2C411A86DF531 CRC64;
MATVTSNASP KSFSFTVSNP FKTLIPNKSP SLCYPTRNKN HHRLGFSIKA TVSTPPSIAT
GNAPSPDYRV EILSESLPFI QKFRGKTIVV KYGGAAMTSP ELKSSVVSDL VLLACVGLRP
ILVHGGGPDI NRYLKQLNIP AEFRDGLRVT DATTMEIVSM VLVGKVNKNL VSLINAAGAT
AVGLSGHDGR LLTARPVPNS AQLGFVGEVA RVDPSVLRPL VDYGYIPVIA SVAADDSGQA
YNINADTVAG ELAAALGAEK LILLTDVAGI LENKEDPSSL IKEIDIKGVK KMIEDGKVAG
GMIPKVKCCI RSLAQGVKTA SIIDGRRQHS LLHEIMSDEG AGTMITG
