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 24-JAN-2024, entry version 123.
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=N-acetyl-L-glutamate 5-phosphotransferase;
DE AltName: Full=NAG kinase;
DE Short=AGK;
DE Flags: Precursor;
GN Name=argC; ORFNames=DDB_G0286257;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; 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., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., 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., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 65-78; 161-172 AND 209-218, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Ura S., Insall R.H.;
RL Submitted (JUL-2009) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate =
CC H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-
CC phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AAFI02000085; EAL64304.1; -; Genomic_DNA.
DR RefSeq; XP_637813.1; XM_632721.1.
DR AlphaFoldDB; Q54M18; -.
DR SMR; Q54M18; -.
DR STRING; 44689.Q54M18; -.
DR PaxDb; 44689-DDB0231462; -.
DR EnsemblProtists; EAL64304; EAL64304; DDB_G0286257.
DR GeneID; 8625527; -.
DR KEGG; ddi:DDB_G0286257; -.
DR dictyBase; DDB_G0286257; argC.
DR eggNOG; KOG2436; Eukaryota.
DR eggNOG; KOG4354; Eukaryota.
DR HOGENOM; CLU_006384_4_0_1; -.
DR InParanoid; Q54M18; -.
DR OMA; IAFIPHV; -.
DR PhylomeDB; Q54M18; -.
DR Reactome; R-DDI-70635; Urea cycle.
DR UniPathway; UPA00068; UER00107.
DR UniPathway; UPA00068; UER00108.
DR PRO; PR:Q54M18; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0003991; F:acetylglutamate kinase activity; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; ISS:dictyBase.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0070401; F:NADP+ binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00150; ArgC_type1; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR000706; AGPR_type-1.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR041734; NAGK-fArgBP.
DR InterPro; IPR011241; NAGK/NAGSA.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR NCBIfam; TIGR00761; argB; 1.
DR NCBIfam; TIGR01850; argC; 1.
DR PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1.
DR PANTHER; PTHR23342:SF0; N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF04768; NAT; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR PIRSF; PIRSF036440; ARG5-6; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01224; ARGC; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Direct protein sequencing; Kinase; Mitochondrion; Multifunctional enzyme;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..847
FT /note="Bifunctional protein argC, mitochondrial"
FT /id="PRO_0000332966"
FT DOMAIN 352..508
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 100..331
FT /note="Acetylglutamate kinase"
FT REGION 531..846
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT ACT_SITE 665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10010"
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
//
