ID ARG56_DICDI Reviewed; 847 AA. AC Q54M18; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 16-JUN-2009, entry version 35. DE RecName: Full=Bifunctional protein argC, mitochondrial; DE Includes: DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase; DE EC=1.2.1.38; DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase; DE Short=NAGSA dehydrogenase; DE Includes: DE RecName: Full=Acetylglutamate kinase; DE EC=2.7.2.8; DE AltName: Full=NAG kinase; DE Short=AGK; DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase; DE Flags: Precursor; GN Name=argC; ORFNames=DDB_G0286257; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., RA Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., RA Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). CC -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) CC + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L- CC glutamate 5-phosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 2/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 3/4. CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the CC acetylglutamate kinase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAFI02000085; EAL64304.1; -; Genomic_DNA. DR RefSeq; XP_637813.1; -. DR GeneID; 3389385; -. DR KEGG; ddi:DDB_0231462; -. DR dictyBase; DDB_G0286257; argC. DR OMA; Q54M18; WVMALPN. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase...; IEA:EC. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR004662; AcgluKinase. DR InterPro; IPR000706; AGPR_act_site. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR011241; NAGK_NAGSA. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_C. DR Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF036440; ARG5-6; 1. DR ProDom; PD003765; AGPR_act_site; 1. DR TIGRFAMs; TIGR00761; argB; 1. DR TIGRFAMs; TIGR01850; argC; 1. DR PROSITE; PS01224; ARGC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Kinase; Mitochondrion; Multifunctional enzyme; KW NADP; Nucleotide-binding; Oxidoreductase; Transferase; KW Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 847 Bifunctional protein argC, mitochondrial. FT /FTId=PRO_0000332966. FT REGION 100 331 Acetylglutamate kinase. FT REGION 531 846 N-acetyl-gamma-glutamyl-phosphate FT reductase. FT COMPBIAS 33 38 Poly-Ser. FT COMPBIAS 66 69 Poly-Ser. FT COMPBIAS 426 429 Poly-Phe. FT ACT_SITE 665 665 By similarity. SQ SEQUENCE 847 AA; 92818 MW; 94C780A710C5B3FB CRC64; MLRNSNKLIK SVIKNESTLL KCKNNNQRVV NYSSSSTSIT SGNGIYSQIK KIEEFVSKKP SVTKVSSSSA TINFNTSKSG STNTTAVDYS KSVKIKDQKQ IVLVKIGGGV IESDISSLIG SLNFLKKIGL FPIVVHGGGP QLNAELAAAG EPAEYVEGLR VTPPSVLAIA QRVFLRENLK IVEALESSGT KARPVTQGVY QATPLDPKLY GFVGNVTKIH TDALASCITN DYVPVISSLA MTPEGQVLNI NADVAALELA KSINPLKILF INTTAGMKDG DGKVMQHIKL DEQYADLMKQ PWVKHGTKLK LKEFKSCLDV LPPSTSITIT SPDLLMKELF AKDGSGTTVE RGEVMHSHES PSFDETKFFA LIEKSTGTKG GRIDYQQLKT DLSKGVVKAF VNSHYTAGIL VRPLSSGSSV SYVDQFFFFN NSIQSTEDSE SVFKKMFENS SYIWKESSNN QLNNEWFKKI ATGFITGATN NIFWTNIDTN KIENSIKECL SQSSTYLSGI TKAASSKSAS EKLLQDKNHK FRVGLIGARG FTGGNLVRLI DGHPNLELAI ASSSTNFGKP ITTEFPQLKS NLKFDNVKPE NIDIFTRDHG IDGWFMALPD KISSPYIQTL ENSSESPVLV DLSSDHRFNE KWTYGQPETN RAAIKESKLI ANPGCYATGM FLTLKPFVND LVTPPSCFGI SGYSGAGSKP SEKNDPTRLS DNILPYKLVQ HTHELEVSHQ LGSPIYFMPH VGQFFQGITL TISMELKYPM TKEQVVERYQ KFYQNEPLIK IDKDGIPEVK SNSGKHTVTI GGFAVNGNHL VVVTTLDNLL KGAATQALQN MNICLGLDEL ASIKNEL //