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Protein

Protein ARG5,6, mitochondrial

Gene

ARG5,6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate.

Enzyme regulationi

The kinase activity is inhibited by arginine.

Pathwayi: L-arginine biosynthesis

This protein is involved in step 2 and 3 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Amino-acid acetyltransferase, mitochondrial (ARG2), Arginine biosynthesis bifunctional protein ArgJ, mitochondrial (ARG7)
  2. Protein ARG5,6, mitochondrial (ARG5,6)
  3. Protein ARG5,6, mitochondrial (ARG5,6)
  4. Acetylornithine aminotransferase, mitochondrial (ARG8)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei675PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • arginine biosynthetic process Source: SGD
  • ornithine biosynthetic process Source: SGD
  • regulation of transcription, DNA-templated Source: SGD

Keywords - Molecular functioni

Kinase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YER069W-MONOMER.
BRENDAi2.7.2.8. 984.
ReactomeiR-SCE-70635. Urea cycle.
UniPathwayiUPA00068; UER00107.
UPA00068; UER00108.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ARG5,6, mitochondrial
Cleaved into the following 2 chains:
Alternative name(s):
N-acetyl-glutamate semialdehyde dehydrogenase
Short name:
NAGSA dehydrogenase
Alternative name(s):
N-acetyl-L-glutamate 5-phosphotransferase
NAG kinase
Short name:
AGK
Gene namesi
Name:ARG5,6
Ordered Locus Names:YER069W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER069W.
SGDiS000000871. ARG5,6.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: SGD

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 65MitochondrionSequence analysisAdd BLAST65
ChainiPRO_000000207366 – 532Acetylglutamate kinaseSequence analysisAdd BLAST467
ChainiPRO_0000002074533 – 863N-acetyl-gamma-glutamyl-phosphate reductaseSequence analysisAdd BLAST331

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei359PhosphoserineCombined sources1

Post-translational modificationi

The protein precursor is cleaved into the two biologically active enzymes, the kinase and the reductase.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ01217.
PRIDEiQ01217.

PTM databases

iPTMnetiQ01217.

Interactioni

Protein-protein interaction databases

BioGridi36812. 15 interactors.
DIPiDIP-5348N.
IntActiQ01217. 3 interactors.
MINTiMINT-492634.

Structurei

Secondary structure

1863
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi68 – 75Combined sources8
Helixi81 – 92Combined sources12
Beta strandi100 – 104Combined sources5
Helixi106 – 111Combined sources6
Helixi113 – 125Combined sources13
Beta strandi130 – 134Combined sources5
Helixi137 – 146Combined sources10
Helixi162 – 185Combined sources24
Beta strandi190 – 193Combined sources4
Beta strandi195 – 203Combined sources9
Helixi205 – 208Combined sources4
Beta strandi209 – 217Combined sources9
Helixi220 – 228Combined sources9
Beta strandi231 – 234Combined sources4
Beta strandi237 – 239Combined sources3
Beta strandi244 – 247Combined sources4
Helixi250 – 261Combined sources12
Beta strandi264 – 269Combined sources6
Beta strandi271 – 274Combined sources4
Turni278 – 281Combined sources4
Beta strandi286 – 288Combined sources3
Helixi289 – 297Combined sources9
Beta strandi300 – 302Combined sources3
Helixi304 – 319Combined sources16
Beta strandi326 – 329Combined sources4
Helixi331 – 333Combined sources3
Helixi334 – 339Combined sources6
Beta strandi340 – 342Combined sources3
Beta strandi345 – 349Combined sources5
Beta strandi355 – 359Combined sources5
Helixi360 – 362Combined sources3
Helixi366 – 373Combined sources8
Turni377 – 379Combined sources3
Beta strandi380 – 384Combined sources5
Helixi386 – 394Combined sources9
Beta strandi398 – 402Combined sources5
Beta strandi407 – 413Combined sources7
Beta strandi415 – 418Combined sources4
Beta strandi420 – 426Combined sources7
Helixi428 – 432Combined sources5
Helixi435 – 446Combined sources12
Beta strandi448 – 455Combined sources8
Helixi461 – 467Combined sources7
Beta strandi469 – 474Combined sources6
Beta strandi477 – 483Combined sources7
Helixi487 – 499Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZZFX-ray2.20A/B/C/D58-356[»]
3ZZGX-ray2.95A/B/C/D58-356[»]
3ZZHX-ray2.10A/B/C/D58-356[»]
3ZZIX-ray3.80A/B/C/D/E/F/G/H58-513[»]
4AB7X-ray3.25A/B/C/D/E/F/G/H58-513[»]
ProteinModelPortaliQ01217.
SMRiQ01217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini353 – 505N-acetyltransferasePROSITE-ProRule annotationAdd BLAST153

Sequence similaritiesi

In the N-terminal section; belongs to the acetylglutamate kinase family.Curated
In the C-terminal section; belongs to the NAGSA dehydrogenase family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000005602.
HOGENOMiHOG000201928.
InParanoidiQ01217.
KOiK12659.
OMAiDENRAWH.
OrthoDBiEOG092C2W4A.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR004662. AcgluKinase.
IPR023013. AGPR_AS.
IPR000706. AGPR_type-1.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR016040. NAD(P)-bd_dom.
IPR011241. NAGK_NAGSA.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
IPR006855. Vertebrate-like_GNAT_dom.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF04768. NAT. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFiPIRSF036440. ARG5-6. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.
TIGR01850. argC. 1 hit.
PROSITEiPS01224. ARGC. 1 hit.
PS51731. GNAT_NAGS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01217-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSASLLVST KRLNASKFQK FVSSLNKSTI AGFASVPLRA PPSVAFTRKK
60 70 80 90 100
VGYSKRYVSS TNGFSATRST VIQLLNNIST KREVEQYLKY FTSVSQQQFA
110 120 130 140 150
VIKVGGAIIS DNLHELASCL AFLYHVGLYP IVLHGTGPQV NGRLEAQGIE
160 170 180 190 200
PDYIDGIRIT DEHTMAVVRK CFLEQNLKLV TALEQLGVRA RPITSGVFTA
210 220 230 240 250
DYLDKDKYKL VGNIKSVTKE PIEASIKAGA LPILTSLAET ASGQMLNVNA
260 270 280 290 300
DVAAGELARV FEPLKIVYLN EKGGIINGST GEKISMINLD EEYDDLMKQS
310 320 330 340 350
WVKYGTKLKI REIKELLDYL PRSSSVAIIN VQDLQKELFT DSGAGTMIRR
360 370 380 390 400
GYKLVKRSSI GEFPSADALR KALQRDAGIS SGKESVASYL RYLENSDFVS
410 420 430 440 450
YADEPLEAVA IVKKDTNVPT LDKFVCSDAA WLNNVTDNVF NVLRRDFPAL
460 470 480 490 500
QWVVSENDAN IAWHFDKSQG SYLKGGKVLF WYGIDDINTI SELVENFVKS
510 520 530 540 550
CDTASTLNSS ASSGVFANKK SARSYSTRST PRPEGVNTNP GRVALIGARG
560 570 580 590 600
YTGKNLVSLI NGHPYLEVAH VSSRELKGQK LQDYTKSEII YESLQIQDIR
610 620 630 640 650
KLEEQNAVDF WVMALPNKVC EPFVETIQSV HGKSKIIDLS ADHRFVSESD
660 670 680 690 700
WAYGLPELND RAKIANAAKI ANPGCYATGS QLTISPLTKY INGLPTVFGV
710 720 730 740 750
SGYSGAGTKP SPKNDPKFLN NNLIPYALSD HIHEREISAR IGHNVAFMPH
760 770 780 790 800
VGQWFQGISL TVSIPIKKGS LSIDEIRKLY RNFYEDEKLV HVIDDIPLVK
810 820 830 840 850
DIEGTHGVVI GGFKLNDAED RVVVCATIDN LLKGAATQCL QNINLAMGYG
860
EYAGIPENKI IGV
Length:863
Mass (Da):94,869
Last modified:April 1, 1993 - v1
Checksum:i21C6AFFC5DAFFF34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57017 Genomic DNA. Translation: CAA40336.1.
U18813 Genomic DNA. Translation: AAB64605.1.
BK006939 Genomic DNA. Translation: DAA07728.1.
PIRiS16807.
RefSeqiNP_010992.1. NM_001178960.1.

Genome annotation databases

EnsemblFungiiYER069W; YER069W; YER069W.
GeneIDi856800.
KEGGisce:YER069W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57017 Genomic DNA. Translation: CAA40336.1.
U18813 Genomic DNA. Translation: AAB64605.1.
BK006939 Genomic DNA. Translation: DAA07728.1.
PIRiS16807.
RefSeqiNP_010992.1. NM_001178960.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZZFX-ray2.20A/B/C/D58-356[»]
3ZZGX-ray2.95A/B/C/D58-356[»]
3ZZHX-ray2.10A/B/C/D58-356[»]
3ZZIX-ray3.80A/B/C/D/E/F/G/H58-513[»]
4AB7X-ray3.25A/B/C/D/E/F/G/H58-513[»]
ProteinModelPortaliQ01217.
SMRiQ01217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36812. 15 interactors.
DIPiDIP-5348N.
IntActiQ01217. 3 interactors.
MINTiMINT-492634.

PTM databases

iPTMnetiQ01217.

Proteomic databases

MaxQBiQ01217.
PRIDEiQ01217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER069W; YER069W; YER069W.
GeneIDi856800.
KEGGisce:YER069W.

Organism-specific databases

EuPathDBiFungiDB:YER069W.
SGDiS000000871. ARG5,6.

Phylogenomic databases

GeneTreeiENSGT00390000005602.
HOGENOMiHOG000201928.
InParanoidiQ01217.
KOiK12659.
OMAiDENRAWH.
OrthoDBiEOG092C2W4A.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00107.
UPA00068; UER00108.
BioCyciYEAST:YER069W-MONOMER.
BRENDAi2.7.2.8. 984.
ReactomeiR-SCE-70635. Urea cycle.

Miscellaneous databases

PROiQ01217.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR004662. AcgluKinase.
IPR023013. AGPR_AS.
IPR000706. AGPR_type-1.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR016040. NAD(P)-bd_dom.
IPR011241. NAGK_NAGSA.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
IPR006855. Vertebrate-like_GNAT_dom.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF04768. NAT. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFiPIRSF036440. ARG5-6. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.
TIGR01850. argC. 1 hit.
PROSITEiPS01224. ARGC. 1 hit.
PS51731. GNAT_NAGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARG56_YEAST
AccessioniPrimary (citable) accession number: Q01217
Secondary accession number(s): D3DLX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 2, 2016
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1180 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.