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)
     (NAG kinase)
     (AGK)
     (N-acetyl-L-glutamate 5-phosphotransferase)

Gene name

	Name:	argC
	ORFNames:	DDB_G0286257

From

Dictyostelium discoideum (Slime mold)

[TaxID: 44689]

Taxonomy

Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan]
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).

Comments

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.
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 (By similarity).
SIMILARITY: In the N-terminal section; belongs to the acetylglutamate kinase family.
SIMILARITY: In the C-terminal section; belongs to the NAGSA dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AAFI02000085; EAL64304.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_637813.1; -.

3D structure databases

ModBase

Q54M18.

Organism-specific databases

dictyBase

DDB_G0286257; argC.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from InterPro).
GO:0003991;	Molecular function: acetylglutamate kinase activity (inferred from electronic annotation from InterPro).
GO:0003942;	Molecular function: N-acetyl-gamma-glutamyl-phosphate reductase activity (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0046983;	Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0006526;	Biological process: arginine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR004662; AcgluKinase.
IPR000706; AGPR_act_site.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR000886; ER_targeting_sequence.
IPR011241; NAGK_NAGSA.
IPR000534; Semialdehyde_DHase_NAD-bd.
IPR012280; Semialdhyde_DHase_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1160.10; Aa_kinase; 1.

Pfam

PF00696; AA_kinase; 1.
PF01118; Semialdhyde_dh; 1.
PF02774; Semialdhyde_dhC; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036440; ARG5-6; 1.

ProDom

PD003765; AGPR_act_site; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00761; argB; 1.
TIGR01850; argC; 1.

PROSITE

PS01224; ARGC; 1.

Genome annotation databases

GeneID

3389385; -.

KEGG

ddi:DDB_0231462; -.

Other

ProtoNet

Q54M18.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Kinase; Mitochondrion; Multifunctional enzyme; NADP; Oxidoreductase; Transferase; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 847`		`Bifunctional protein argC, mitochondrial.`	`PRO_0000332966`
`REGION`	`100 331`	`232`	`Acetylglutamate kinase.`
`REGION`	`531 846`	`316`	`N-acetyl-gamma-glutamyl-phosphate reductase.`
`COMPBIAS`	`33 38`	`6`	`Poly-Ser.`
`COMPBIAS`	`66 69`	`4`	`Poly-Ser.`
`COMPBIAS`	`426 429`	`4`	`Poly-Phe.`
`ACT_SITE`	`665 665`		`By similarity.`

Sequence information

Length: 847 AA [This is the length of the unprocessed precursor]

Molecular weight: 92818 Da [This is the MW of the unprocessed precursor]

CRC64: 94C780A710C5B3FB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLRNSNKLIK SVIKNESTLL KCKNNNQRVV NYSSSSTSIT SGNGIYSQIK KIEEFVSKKP 

        70         80         90        100        110        120 
SVTKVSSSSA TINFNTSKSG STNTTAVDYS KSVKIKDQKQ IVLVKIGGGV IESDISSLIG 

       130        140        150        160        170        180 
SLNFLKKIGL FPIVVHGGGP QLNAELAAAG EPAEYVEGLR VTPPSVLAIA QRVFLRENLK 

       190        200        210        220        230        240 
IVEALESSGT KARPVTQGVY QATPLDPKLY GFVGNVTKIH TDALASCITN DYVPVISSLA 

       250        260        270        280        290        300 
MTPEGQVLNI NADVAALELA KSINPLKILF INTTAGMKDG DGKVMQHIKL DEQYADLMKQ 

       310        320        330        340        350        360 
PWVKHGTKLK LKEFKSCLDV LPPSTSITIT SPDLLMKELF AKDGSGTTVE RGEVMHSHES 

       370        380        390        400        410        420 
PSFDETKFFA LIEKSTGTKG GRIDYQQLKT DLSKGVVKAF VNSHYTAGIL VRPLSSGSSV 

       430        440        450        460        470        480 
SYVDQFFFFN NSIQSTEDSE SVFKKMFENS SYIWKESSNN QLNNEWFKKI ATGFITGATN 

       490        500        510        520        530        540 
NIFWTNIDTN KIENSIKECL SQSSTYLSGI TKAASSKSAS EKLLQDKNHK FRVGLIGARG 

       550        560        570        580        590        600 
FTGGNLVRLI DGHPNLELAI ASSSTNFGKP ITTEFPQLKS NLKFDNVKPE NIDIFTRDHG 

       610        620        630        640        650        660 
IDGWFMALPD KISSPYIQTL ENSSESPVLV DLSSDHRFNE KWTYGQPETN RAAIKESKLI 

       670        680        690        700        710        720 
ANPGCYATGM FLTLKPFVND LVTPPSCFGI SGYSGAGSKP SEKNDPTRLS DNILPYKLVQ 

       730        740        750        760        770        780 
HTHELEVSHQ LGSPIYFMPH VGQFFQGITL TISMELKYPM TKEQVVERYQ KFYQNEPLIK 

       790        800        810        820        830        840 
IDKDGIPEVK SNSGKHTVTI GGFAVNGNHL VVVTTLDNLL KGAATQALQN MNICLGLDEL 


ASIKNEL

Q54M18 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools