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Protein ARG5,6, mitochondrial [Cleaved into: N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) (N-acetyl-glutamate semialdehyde dehydrogenase) (NAGSA dehydrogenase); Acetylglutamate kinase (EC 2.7.2.8) (N-acetyl-L-glutamate 5-phosphotransferase) (NAG kinase) (AGK)]

 ARG56_YEAST             Reviewed;         863 AA.
Q01217; D3DLX4;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
20-JUN-2018, entry version 182.
RecName: Full=Protein ARG5,6, mitochondrial;
Contains:
RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase;
EC=1.2.1.38;
AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase;
Short=NAGSA dehydrogenase;
Contains:
RecName: Full=Acetylglutamate kinase;
EC=2.7.2.8;
AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase;
AltName: Full=NAG kinase;
Short=AGK;
Flags: Precursor;
Name=ARG5,6; OrderedLocusNames=YER069W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sigma 1278B;
PubMed=1851947; DOI=10.1007/BF00273599;
Boonchird C., Messenguy F., Dubois E.;
"Characterization of the yeast ARG5,6 gene: determination of the
nucleotide sequence, analysis of the control region and of ARG5,6
transcript.";
Mol. Gen. Genet. 226:154-166(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PROTEOLYTIC PROCESSING.
PubMed=1649049; DOI=10.1111/j.1432-1033.1991.tb16128.x;
Boonchird C., Messenguy F., Dubois E.;
"Determination of amino acid sequences involved in the processing of
the ARG5/ARG6 precursor in Saccharomyces cerevisiae.";
Eur. J. Biochem. 199:325-335(1991).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+)
+ phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
-!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-
glutamate 5-phosphate.
-!- ENZYME REGULATION: The kinase activity is inhibited by arginine.
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
acetyl-L-ornithine from L-glutamate: step 2/4.
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
acetyl-L-ornithine from L-glutamate: step 3/4.
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- PTM: The protein precursor is cleaved into the two biologically
active enzymes, the kinase and the reductase.
{ECO:0000269|PubMed:1649049}.
-!- MISCELLANEOUS: Present with 1180 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: In the N-terminal section; belongs to the
acetylglutamate kinase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
dehydrogenase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X57017; CAA40336.1; -; Genomic_DNA.
EMBL; U18813; AAB64605.1; -; Genomic_DNA.
EMBL; BK006939; DAA07728.1; -; Genomic_DNA.
PIR; S16807; S16807.
RefSeq; NP_010992.1; NM_001178960.1.
PDB; 3ZZF; X-ray; 2.20 A; A/B/C/D=58-356.
PDB; 3ZZG; X-ray; 2.95 A; A/B/C/D=58-356.
PDB; 3ZZH; X-ray; 2.10 A; A/B/C/D=58-356.
PDB; 3ZZI; X-ray; 3.80 A; A/B/C/D/E/F/G/H=58-513.
PDB; 4AB7; X-ray; 3.25 A; A/B/C/D/E/F/G/H=58-513.
PDBsum; 3ZZF; -.
PDBsum; 3ZZG; -.
PDBsum; 3ZZH; -.
PDBsum; 3ZZI; -.
PDBsum; 4AB7; -.
ProteinModelPortal; Q01217; -.
SMR; Q01217; -.
BioGrid; 36812; 21.
ComplexPortal; CPX-1151; N-acetylglutamate synthase NAGS/NAGK complex.
DIP; DIP-5348N; -.
IntAct; Q01217; 3.
MINT; Q01217; -.
STRING; 4932.YER069W; -.
MoonProt; Q01217; -.
iPTMnet; Q01217; -.
MaxQB; Q01217; -.
PaxDb; Q01217; -.
PRIDE; Q01217; -.
EnsemblFungi; YER069W; YER069W; YER069W.
GeneID; 856800; -.
KEGG; sce:YER069W; -.
EuPathDB; FungiDB:YER069W; -.
SGD; S000000871; ARG5,6.
GeneTree; ENSGT00390000005602; -.
HOGENOM; HOG000201928; -.
InParanoid; Q01217; -.
KO; K12659; -.
OMA; DENRAWH; -.
OrthoDB; EOG092C2W4A; -.
BioCyc; YEAST:YER069W-MONOMER; -.
BRENDA; 2.7.2.8; 984.
Reactome; R-SCE-70635; Urea cycle.
UniPathway; UPA00068; UER00107.
UniPathway; UPA00068; UER00108.
PRO; PR:Q01217; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central.
GO; GO:0003991; F:acetylglutamate kinase activity; IDA:SGD.
GO; GO:0034618; F:arginine binding; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IDA:SGD.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0006526; P:arginine biosynthetic process; TAS:SGD.
GO; GO:0006592; P:ornithine biosynthetic process; TAS:SGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
Gene3D; 3.40.1160.10; -; 1.
HAMAP; MF_00150; ArgC_type1; 1.
InterPro; IPR036393; AceGlu_kinase-like_sf.
InterPro; IPR004662; AcgluKinase_fam.
InterPro; IPR023013; AGPR_AS.
InterPro; IPR000706; AGPR_type-1.
InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR011241; NAGK/NAGSA.
InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
InterPro; IPR006855; Vertebrate-like_GNAT_dom.
Pfam; PF00696; AA_kinase; 1.
Pfam; PF04768; NAT; 1.
Pfam; PF01118; Semialdhyde_dh; 1.
Pfam; PF02774; Semialdhyde_dhC; 1.
PIRSF; PIRSF036440; ARG5-6; 1.
SMART; SM00859; Semialdhyde_dh; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF53633; SSF53633; 1.
TIGRFAMs; TIGR00761; argB; 1.
TIGRFAMs; TIGR01850; argC; 1.
PROSITE; PS01224; ARGC; 1.
PROSITE; PS51731; GNAT_NAGS; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis; Arginine biosynthesis;
ATP-binding; Complete proteome; Kinase; Mitochondrion;
Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase;
Phosphoprotein; Reference proteome; Transferase; Transit peptide.
TRANSIT 1 65 Mitochondrion. {ECO:0000255}.
CHAIN 66 532 Acetylglutamate kinase. {ECO:0000255}.
/FTId=PRO_0000002073.
CHAIN 533 863 N-acetyl-gamma-glutamyl-phosphate
reductase. {ECO:0000255}.
/FTId=PRO_0000002074.
DOMAIN 353 505 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
ACT_SITE 675 675 {ECO:0000255|PROSITE-ProRule:PRU10010}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
HELIX 68 75 {ECO:0000244|PDB:3ZZH}.
HELIX 81 92 {ECO:0000244|PDB:3ZZH}.
STRAND 100 104 {ECO:0000244|PDB:3ZZH}.
HELIX 106 111 {ECO:0000244|PDB:3ZZH}.
HELIX 113 125 {ECO:0000244|PDB:3ZZH}.
STRAND 130 134 {ECO:0000244|PDB:3ZZH}.
HELIX 137 146 {ECO:0000244|PDB:3ZZH}.
HELIX 162 185 {ECO:0000244|PDB:3ZZH}.
STRAND 190 193 {ECO:0000244|PDB:3ZZH}.
STRAND 195 203 {ECO:0000244|PDB:3ZZH}.
HELIX 205 208 {ECO:0000244|PDB:3ZZH}.
STRAND 209 217 {ECO:0000244|PDB:3ZZH}.
HELIX 220 228 {ECO:0000244|PDB:3ZZH}.
STRAND 231 234 {ECO:0000244|PDB:3ZZH}.
STRAND 237 239 {ECO:0000244|PDB:3ZZG}.
STRAND 244 247 {ECO:0000244|PDB:3ZZH}.
HELIX 250 261 {ECO:0000244|PDB:3ZZH}.
STRAND 264 269 {ECO:0000244|PDB:3ZZH}.
STRAND 271 274 {ECO:0000244|PDB:3ZZF}.
TURN 278 281 {ECO:0000244|PDB:3ZZH}.
STRAND 286 288 {ECO:0000244|PDB:3ZZH}.
HELIX 289 297 {ECO:0000244|PDB:3ZZH}.
STRAND 300 302 {ECO:0000244|PDB:3ZZG}.
HELIX 304 319 {ECO:0000244|PDB:3ZZH}.
STRAND 326 329 {ECO:0000244|PDB:3ZZH}.
HELIX 331 333 {ECO:0000244|PDB:3ZZH}.
HELIX 334 339 {ECO:0000244|PDB:3ZZH}.
STRAND 340 342 {ECO:0000244|PDB:4AB7}.
STRAND 345 349 {ECO:0000244|PDB:3ZZH}.
STRAND 355 359 {ECO:0000244|PDB:4AB7}.
HELIX 360 362 {ECO:0000244|PDB:4AB7}.
HELIX 366 373 {ECO:0000244|PDB:4AB7}.
TURN 377 379 {ECO:0000244|PDB:4AB7}.
STRAND 380 384 {ECO:0000244|PDB:4AB7}.
HELIX 386 394 {ECO:0000244|PDB:4AB7}.
STRAND 398 402 {ECO:0000244|PDB:4AB7}.
STRAND 407 413 {ECO:0000244|PDB:4AB7}.
STRAND 415 418 {ECO:0000244|PDB:4AB7}.
STRAND 420 426 {ECO:0000244|PDB:4AB7}.
HELIX 428 432 {ECO:0000244|PDB:4AB7}.
HELIX 435 446 {ECO:0000244|PDB:4AB7}.
STRAND 448 455 {ECO:0000244|PDB:4AB7}.
HELIX 461 467 {ECO:0000244|PDB:4AB7}.
STRAND 469 474 {ECO:0000244|PDB:4AB7}.
STRAND 477 483 {ECO:0000244|PDB:4AB7}.
HELIX 487 499 {ECO:0000244|PDB:4AB7}.
SEQUENCE 863 AA; 94869 MW; 21C6AFFC5DAFFF34 CRC64;
MPSASLLVST KRLNASKFQK FVSSLNKSTI AGFASVPLRA PPSVAFTRKK VGYSKRYVSS
TNGFSATRST VIQLLNNIST KREVEQYLKY FTSVSQQQFA VIKVGGAIIS DNLHELASCL
AFLYHVGLYP IVLHGTGPQV NGRLEAQGIE PDYIDGIRIT DEHTMAVVRK CFLEQNLKLV
TALEQLGVRA RPITSGVFTA DYLDKDKYKL VGNIKSVTKE PIEASIKAGA LPILTSLAET
ASGQMLNVNA DVAAGELARV FEPLKIVYLN EKGGIINGST GEKISMINLD EEYDDLMKQS
WVKYGTKLKI REIKELLDYL PRSSSVAIIN VQDLQKELFT DSGAGTMIRR GYKLVKRSSI
GEFPSADALR KALQRDAGIS SGKESVASYL RYLENSDFVS YADEPLEAVA IVKKDTNVPT
LDKFVCSDAA WLNNVTDNVF NVLRRDFPAL QWVVSENDAN IAWHFDKSQG SYLKGGKVLF
WYGIDDINTI SELVENFVKS CDTASTLNSS ASSGVFANKK SARSYSTRST PRPEGVNTNP
GRVALIGARG YTGKNLVSLI NGHPYLEVAH VSSRELKGQK LQDYTKSEII YESLQIQDIR
KLEEQNAVDF WVMALPNKVC EPFVETIQSV HGKSKIIDLS ADHRFVSESD WAYGLPELND
RAKIANAAKI ANPGCYATGS QLTISPLTKY INGLPTVFGV SGYSGAGTKP SPKNDPKFLN
NNLIPYALSD HIHEREISAR IGHNVAFMPH VGQWFQGISL TVSIPIKKGS LSIDEIRKLY
RNFYEDEKLV HVIDDIPLVK DIEGTHGVVI GGFKLNDAED RVVVCATIDN LLKGAATQCL
QNINLAMGYG EYAGIPENKI IGV


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