| Tag | Content |
|---|
| CPLM ID | CPLM-010838 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein ARG5,6, mitochondrial |
Protein Synonyms/Alias | N-acetyl-gamma-glutamyl-phosphate reductase; N-acetyl-glutamate semialdehyde dehydrogenase; NAGSA dehydrogenase; Acetylglutamate kinase; N-acetyl-L-glutamate 5-phosphotransferase; NAG kinase; AGK |
Gene Name | ARG5,6 |
Gene Synonyms/Alias | YER069W |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 205 | FTADYLDKDKYKLVG | acetylation | [1] | | 272 | KIVYLNEKGGIINGS | acetylation | [1] | | 303 | LMKQSWVKYGTKLKI | acetylation | [1] | | 709 | GYSGAGTKPSPKNDP | acetylation | [1] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | |
Sequence Annotation | ACT_SITE 675 675 By similarity.
MOD_RES 359 359 Phosphoserine. |
Keyword | 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. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 863 AA |
Protein Sequence | MPSASLLVST KRLNASKFQK FVSSLNKSTI AGFASVPLRA PPSVAFTRKK VGYSKRYVSS 60
TNGFSATRST VIQLLNNIST KREVEQYLKY FTSVSQQQFA VIKVGGAIIS DNLHELASCL 120
AFLYHVGLYP IVLHGTGPQV NGRLEAQGIE PDYIDGIRIT DEHTMAVVRK CFLEQNLKLV 180
TALEQLGVRA RPITSGVFTA DYLDKDKYKL VGNIKSVTKE PIEASIKAGA LPILTSLAET 240
ASGQMLNVNA DVAAGELARV FEPLKIVYLN EKGGIINGST GEKISMINLD EEYDDLMKQS 300
WVKYGTKLKI REIKELLDYL PRSSSVAIIN VQDLQKELFT DSGAGTMIRR GYKLVKRSSI 360
GEFPSADALR KALQRDAGIS SGKESVASYL RYLENSDFVS YADEPLEAVA IVKKDTNVPT 420
LDKFVCSDAA WLNNVTDNVF NVLRRDFPAL QWVVSENDAN IAWHFDKSQG SYLKGGKVLF 480
WYGIDDINTI SELVENFVKS CDTASTLNSS ASSGVFANKK SARSYSTRST PRPEGVNTNP 540
GRVALIGARG YTGKNLVSLI NGHPYLEVAH VSSRELKGQK LQDYTKSEII YESLQIQDIR 600
KLEEQNAVDF WVMALPNKVC EPFVETIQSV HGKSKIIDLS ADHRFVSESD WAYGLPELND 660
RAKIANAAKI ANPGCYATGS QLTISPLTKY INGLPTVFGV SGYSGAGTKP SPKNDPKFLN 720
NNLIPYALSD HIHEREISAR IGHNVAFMPH VGQWFQGISL TVSIPIKKGS LSIDEIRKLY 780
RNFYEDEKLV HVIDDIPLVK DIEGTHGVVI GGFKLNDAED RVVVCATIDN LLKGAATQCL 840
QNINLAMGYG EYAGIPENKI IGV 863 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IDA:SGD. GO:0003991; F:acetylglutamate kinase activity; IDA:SGD. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IDA:SGD. GO:0051287; F:NAD binding; IEA:InterPro. GO:0006526; P:arginine biosynthetic process; TAS:SGD. GO:0006592; P:ornithine biosynthetic process; TAS:SGD. GO:0006355; P:regulation of transcription, DNA-dependent; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |