Q54M18 (ARG56_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein argC, mitochondrial

Including the following 2 domains:

1. N-acetyl-gamma-glutamyl-phosphate reductase
   EC=1.2.1.38
   Alternative name(s):
   N-acetyl-glutamate semialdehyde dehydrogenase
   Short name=NAGSA dehydrogenase
2. Acetylglutamate kinase
   EC=2.7.2.8
   Alternative name(s):
   N-acetyl-L-glutamate 5-phosphotransferase
   NAG kinase
   Short name=AGK

Gene names

Name:	argC
ORF Names:	DDB_G0286257

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	847 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	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.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	In the N-terminal section; belongs to the acetylglutamate kinase family. In the C-terminal section; belongs to the NAGSA dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Kinase Oxidoreductase Transferase
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	arginine biosynthetic process Inferred from sequence or structural similarity. Source: dictyBase ornithine biosynthetic process Inferred from sequence or structural similarity. Source: dictyBase
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from sequence or structural similarity. Source: dictyBase NAD binding Inferred from electronic annotation. Source: InterPro acetylglutamate kinase activity Inferred from sequence or structural similarity. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 847		Bifunctional protein argC, mitochondrial		PRO_0000332966
Regions
	Region	100 – 331	232	Acetylglutamate kinase
	Region	531 – 846	316	N-acetyl-gamma-glutamyl-phosphate reductase
	Compositional bias	33 – 38	6	Poly-Ser
	Compositional bias	66 – 69	4	Poly-Ser
	Compositional bias	426 – 429	4	Poly-Phe
Sites
	Active site	665	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54M18 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 94C780A710C5B3FB	FASTA	847	92,818
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." 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. Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	Bienvenut W.V., Ura S., Insall R.H. Submitted (JUL-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 65-78; 161-172 AND 209-218, MASS SPECTROMETRY. Strain: AX2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000085 Genomic DNA. Translation: EAL64304.1.
RefSeq	XP_637813.1. XM_632721.1.
3D structure databases
HSSP	HSSP built from PDB template 1VKN based on UniProtKB Q9X2A2.
ProteinModelPortal	Q54M18.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0231462.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0231462; DDB0231462; DDB_G0286257.
GeneID	8625527.
KEGG	ddi:DDB_G0286257.
Organism-specific databases
dictyBase	DDB_G0286257. argC.
Phylogenomic databases
eggNOG	COG0548.
KO	K12659.
OMA	LIGARGY.
Enzyme and pathway databases
UniPathway	UPA00068; UER00107. UPA00068; UER00108.
Family and domain databases
Gene3D	3.40.1160.10. 1 hit. 3.40.50.720. 1 hit.
InterPro	IPR004662. AcgluKinase. IPR023013. AGPR_AS. IPR000706. AGPR_type-1. IPR001048. Asp/Glu/Uridylate_kinase. IPR006855. DUF619. IPR016040. NAD(P)-bd_dom. IPR011241. NAGK_NAGSA. IPR000534. Semialdehyde_DH_NAD-bd. [Graphical view]
Pfam	PF00696. AA_kinase. 1 hit. PF04768. DUF619. 1 hit. PF01118. Semialdhyde_dh. 1 hit. [Graphical view]
PIRSF	PIRSF036440. ARG5-6. 1 hit.
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
SUPFAM	SSF53633. Aa_kinase. 1 hit.
TIGRFAMs	TIGR00761. argB. 1 hit. TIGR01850. argC. 1 hit.
PROSITE	PS01224. ARGC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARG56_DICDI

Accession

Primary (citable) accession number: Q54M18

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 24, 2005
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)