ARG56_YEAST
ID ARG56_YEAST Reviewed; 863 AA.
AC Q01217; D3DLX4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Protein ARG5,6, mitochondrial;
DE Contains:
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase;
DE EC=1.2.1.38 {ECO:0000269|PubMed:1851947};
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase;
DE Short=NAGSA dehydrogenase;
DE Contains:
DE RecName: Full=Acetylglutamate kinase;
DE EC=2.7.2.8 {ECO:0000269|PubMed:1851947};
DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase;
DE AltName: Full=NAG kinase;
DE Short=AGK;
DE Flags: Precursor;
GN Name=ARG5,6; OrderedLocusNames=YER069W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=Sigma 1278B;
RX PubMed=1851947; DOI=10.1007/bf00273599;
RA Boonchird C., Messenguy F., Dubois E.;
RT "Characterization of the yeast ARG5,6 gene: determination of the nucleotide
RT sequence, analysis of the control region and of ARG5,6 transcript.";
RL Mol. Gen. Genet. 226:154-166(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEOLYTIC PROCESSING.
RX PubMed=1649049; DOI=10.1111/j.1432-1033.1991.tb16128.x;
RA Boonchird C., Messenguy F., Dubois E.;
RT "Determination of amino acid sequences involved in the processing of the
RT ARG5/ARG6 precursor in Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 199:325-335(1991).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate =
CC H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38;
CC Evidence={ECO:0000269|PubMed:1851947};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21589;
CC Evidence={ECO:0000305|PubMed:1851947};
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:1851947};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14630;
CC Evidence={ECO:0000305|PubMed:1851947};
CC -!- ACTIVITY REGULATION: The kinase activity is inhibited by arginine.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- PTM: The protein precursor is cleaved into the two biologically active
CC enzymes, the kinase and the reductase. {ECO:0000269|PubMed:1649049}.
CC -!- MISCELLANEOUS: Present with 1180 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; X57017; CAA40336.1; -; Genomic_DNA.
DR EMBL; U18813; AAB64605.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07728.1; -; Genomic_DNA.
DR PIR; S16807; S16807.
DR RefSeq; NP_010992.1; NM_001178960.1.
DR PDB; 3ZZF; X-ray; 2.20 A; A/B/C/D=58-356.
DR PDB; 3ZZG; X-ray; 2.95 A; A/B/C/D=58-356.
DR PDB; 3ZZH; X-ray; 2.10 A; A/B/C/D=58-356.
DR PDB; 3ZZI; X-ray; 3.80 A; A/B/C/D/E/F/G/H=58-513.
DR PDB; 4AB7; X-ray; 3.25 A; A/B/C/D/E/F/G/H=58-513.
DR PDBsum; 3ZZF; -.
DR PDBsum; 3ZZG; -.
DR PDBsum; 3ZZH; -.
DR PDBsum; 3ZZI; -.
DR PDBsum; 4AB7; -.
DR AlphaFoldDB; Q01217; -.
DR SMR; Q01217; -.
DR BioGRID; 36812; 26.
DR ComplexPortal; CPX-1151; N-acetylglutamate synthase NAGS/NAGK complex.
DR DIP; DIP-5348N; -.
DR IntAct; Q01217; 3.
DR MINT; Q01217; -.
DR STRING; 4932.YER069W; -.
DR MoonProt; Q01217; -.
DR iPTMnet; Q01217; -.
DR MaxQB; Q01217; -.
DR PaxDb; Q01217; -.
DR PRIDE; Q01217; -.
DR EnsemblFungi; YER069W_mRNA; YER069W; YER069W.
DR GeneID; 856800; -.
DR KEGG; sce:YER069W; -.
DR SGD; S000000871; ARG5,6.
DR VEuPathDB; FungiDB:YER069W; -.
DR eggNOG; KOG2436; Eukaryota.
DR eggNOG; KOG4354; Eukaryota.
DR HOGENOM; CLU_006384_4_0_1; -.
DR InParanoid; Q01217; -.
DR OMA; VWVMALP; -.
DR BioCyc; YEAST:YER069W-MON; -.
DR BRENDA; 2.7.2.8; 984.
DR Reactome; R-SCE-70635; Urea cycle.
DR UniPathway; UPA00068; UER00107.
DR UniPathway; UPA00068; UER00108.
DR PRO; PR:Q01217; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; Q01217; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0106098; C:NAGS/NAGK complex; IPI:ComplexPortal.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IDA:SGD.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006592; P:ornithine biosynthetic process; TAS:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
DR CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR HAMAP; MF_00150; ArgC_type1; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR000706; AGPR_type-1.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR041734; NAGK-fArgBP.
DR InterPro; IPR011241; NAGK/NAGSA.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF04768; NAT; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR PIRSF; PIRSF036440; ARG5-6; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR00761; argB; 1.
DR TIGRFAMs; TIGR01850; argC; 1.
DR PROSITE; PS01224; ARGC; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Kinase; Mitochondrion; Multifunctional enzyme; NADP; Nucleotide-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..65
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 66..532
FT /note="Acetylglutamate kinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002073"
FT CHAIN 533..863
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002074"
FT DOMAIN 353..505
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 675
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10010"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 162..185
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:3ZZG"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 250..261
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:3ZZF"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3ZZG"
FT HELIX 304..319
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:3ZZH"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:4AB7"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:3ZZH"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:4AB7"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:4AB7"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:4AB7"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:4AB7"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:4AB7"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:4AB7"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:4AB7"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:4AB7"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:4AB7"
FT STRAND 420..426
FT /evidence="ECO:0007829|PDB:4AB7"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:4AB7"
FT HELIX 435..446
FT /evidence="ECO:0007829|PDB:4AB7"
FT STRAND 448..455
FT /evidence="ECO:0007829|PDB:4AB7"
FT HELIX 461..467
FT /evidence="ECO:0007829|PDB:4AB7"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:4AB7"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:4AB7"
FT HELIX 487..499
FT /evidence="ECO:0007829|PDB:4AB7"
SQ 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
