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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei675 – 6751PROSITE-ProRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6565MitochondrionSequence analysisAdd
BLAST
Chaini66 – 532467Acetylglutamate kinaseSequence analysisPRO_0000002073Add
BLAST
Chaini533 – 863331N-acetyl-gamma-glutamyl-phosphate reductaseSequence analysisPRO_0000002074Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei359 – 3591PhosphoserineCombined sources

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 interactions.
DIPiDIP-5348N.
IntActiQ01217. 3 interactions.
MINTiMINT-492634.

Structurei

Secondary structure

1
863
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi68 – 758Combined sources
Helixi81 – 9212Combined sources
Beta strandi100 – 1045Combined sources
Helixi106 – 1116Combined sources
Helixi113 – 12513Combined sources
Beta strandi130 – 1345Combined sources
Helixi137 – 14610Combined sources
Helixi162 – 18524Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi195 – 2039Combined sources
Helixi205 – 2084Combined sources
Beta strandi209 – 2179Combined sources
Helixi220 – 2289Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi244 – 2474Combined sources
Helixi250 – 26112Combined sources
Beta strandi264 – 2696Combined sources
Beta strandi271 – 2744Combined sources
Turni278 – 2814Combined sources
Beta strandi286 – 2883Combined sources
Helixi289 – 2979Combined sources
Beta strandi300 – 3023Combined sources
Helixi304 – 31916Combined sources
Beta strandi326 – 3294Combined sources
Helixi331 – 3333Combined sources
Helixi334 – 3396Combined sources
Beta strandi340 – 3423Combined sources
Beta strandi345 – 3495Combined sources
Beta strandi355 – 3595Combined sources
Helixi360 – 3623Combined sources
Helixi366 – 3738Combined sources
Turni377 – 3793Combined sources
Beta strandi380 – 3845Combined sources
Helixi386 – 3949Combined sources
Beta strandi398 – 4025Combined sources
Beta strandi407 – 4137Combined sources
Beta strandi415 – 4184Combined sources
Beta strandi420 – 4267Combined sources
Helixi428 – 4325Combined sources
Helixi435 – 44612Combined sources
Beta strandi448 – 4558Combined sources
Helixi461 – 4677Combined sources
Beta strandi469 – 4746Combined sources
Beta strandi477 – 4837Combined sources
Helixi487 – 49913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 67-502, 542-855.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini353 – 505153N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

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
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. Positions 67-502, 542-855.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36812. 15 interactions.
DIPiDIP-5348N.
IntActiQ01217. 3 interactions.
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: September 7, 2016
This is version 164 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.