ID ARG56_CANAX Reviewed; 857 AA.
AC P78586;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 13-SEP-2023, entry version 111.
DE RecName: Full=Protein ARG5,6, mitochondrial;
DE Contains:
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 Contains:
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=ARG5,6;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 64385 / 1001;
RX PubMed=9043106; DOI=10.1099/00221287-143-2-297;
RA Negredo A., Monteoliva L., Gil C., Pla J., Nombela C.;
RT "Cloning, analysis and one-step disruption of the ARG5,6 gene of Candida
RT albicans.";
RL Microbiology 143:297-302(1997).
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.
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; X98880; CAA67383.1; -; Genomic_DNA.
DR AlphaFoldDB; P78586; -.
DR SMR; P78586; -.
DR VEuPathDB; FungiDB:C1_09290C_A; -.
DR VEuPathDB; FungiDB:CAWG_00500; -.
DR UniPathway; UPA00068; UER00107.
DR UniPathway; UPA00068; UER00108.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR CDD; cd04263; DUF619-NAGK-FABP; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Kinase;
KW Mitochondrion; Multifunctional enzyme; NADP; Nucleotide-binding;
KW Oxidoreductase; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..?529
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000002067"
FT CHAIN ?530..857
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000002068"
FT DOMAIN 341..492
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 509..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 669
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 857 AA; 95067 MW; AE2CEAD8FF8C4C71 CRC64;
MIRQVNKKAI SNSLFKRLSL SGSAFANITA NKKSSTHQLN QKTQLANVRF YSTKSTVIQL
LNNIGSKREV EQYLKYFTSV SQQQFAVIKV GGAIITQQLN ELASCLAFLY HVGLYPIVLH
GTGPQINELL ENEGVEPEYI DGIRITNPKT MEVVRKCFLE QNLRLVTALE KIGVHARPIT
AGVFEAEYLD KDKYQLVGKI TSVNKSPVEA AINSGYLPIL TSLAETSSGQ LLNVNADVAA
GELAREFEPL KIVYLNEKGG IINGNTGEKV SAINLDEEYE DLLKESWVKY GTKLKIKEIH
DLLQHLPRSS SVAIIDVNDL QKELFTDSGA GTLIRRGYRL INRNSLRDFG NPDLLRNALL
RDPEIKTGKV SVASYLKFLD SVQFKSYGDE PLEVLAIVVE QNDKIPKLDE FLSSKTGWLN
NVTDNIFNAI KKDYSQLCWV VNENDANLPW YFSKSDGSFA KNGQILFWYG LNIDEASKLI
KEFDSSSIGS SLSSSKESGV FTSAQQKRGF HHSTVRRNTN PNPPLSEGKQ TERKKVALIG
ARGYTGQNLI KLIDNHPYLD ISYVSSRELE GQKLQGYNKD NIVYSNLQIE DIKRLEENNE
VDVWVMALPN GVCKPFVDTI DLVQNPNSKI VDLSADYRFD TTGEWTYGLP ELNDRKTIAQ
AKKISNPGCY ATAAQVAIAP LKEYISGTPS IFGVSGYSGA GTKPSPKNDV NLLSNNLIPY
SLTDHVHEKE ISSQLGLQVA FTPHVAQWFQ GITHTINIPI KKGSLTSREI RNIYQDRYQG
EKLITISGEA PLVKDISGKH GVVVGGFAVN SNEDRVVIVA TIDNLLKGAA TQCLQNINLS
QEFGEYDGIP TESLIRG
//
