Reviewed, UniProtKB/Swiss-Prot P78586 (ARG56_CANAL)

Names and origin

Protein names

Recommended name:
    Protein ARG5,6, mitochondrial
Cleaved into the following 2 chains:
    1- Recommended name:
            N-acetyl-gamma-glutamyl-phosphate reductase
              EC=1.2.1.38
        Alternative name(s):
            N-acetyl-glutamate semialdehyde dehydrogenase
              Short name=NAGSA dehydrogenase
    2- Recommended name:
            Acetylglutamate kinase
              EC=2.7.2.8
        Alternative name(s):
            NAG kinase
              Short name=AGK
            N-acetyl-L-glutamate 5-phosphotransferase

Gene names

Name:

ARG5,6

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	857 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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.
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	Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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 electronic annotation. Source: EC NAD or NADH binding Inferred from electronic annotation. Source: InterPro acetylglutamate kinase activity Inferred from electronic annotation. Source: EC protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – ?529		Acetylglutamate kinase		PRO_0000002067
	Chain	?530 – 857	328	N-acetyl-gamma-glutamyl-phosphate reductase		PRO_0000002068
Sites
	Active site	669	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P78586-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: AE2CEAD8FF8C4C71	FASTA	857	95,067
	10 20 30 40 50 60 MIRQVNKKAI SNSLFKRLSL SGSAFANITA NKKSSTHQLN QKTQLANVRF YSTKSTVIQL 70 80 90 100 110 120 LNNIGSKREV EQYLKYFTSV SQQQFAVIKV GGAIITQQLN ELASCLAFLY HVGLYPIVLH 130 140 150 160 170 180 GTGPQINELL ENEGVEPEYI DGIRITNPKT MEVVRKCFLE QNLRLVTALE KIGVHARPIT 190 200 210 220 230 240 AGVFEAEYLD KDKYQLVGKI TSVNKSPVEA AINSGYLPIL TSLAETSSGQ LLNVNADVAA 250 260 270 280 290 300 GELAREFEPL KIVYLNEKGG IINGNTGEKV SAINLDEEYE DLLKESWVKY GTKLKIKEIH 310 320 330 340 350 360 DLLQHLPRSS SVAIIDVNDL QKELFTDSGA GTLIRRGYRL INRNSLRDFG NPDLLRNALL 370 380 390 400 410 420 RDPEIKTGKV SVASYLKFLD SVQFKSYGDE PLEVLAIVVE QNDKIPKLDE FLSSKTGWLN 430 440 450 460 470 480 NVTDNIFNAI KKDYSQLCWV VNENDANLPW YFSKSDGSFA KNGQILFWYG LNIDEASKLI 490 500 510 520 530 540 KEFDSSSIGS SLSSSKESGV FTSAQQKRGF HHSTVRRNTN PNPPLSEGKQ TERKKVALIG 550 560 570 580 590 600 ARGYTGQNLI KLIDNHPYLD ISYVSSRELE GQKLQGYNKD NIVYSNLQIE DIKRLEENNE 610 620 630 640 650 660 VDVWVMALPN GVCKPFVDTI DLVQNPNSKI VDLSADYRFD TTGEWTYGLP ELNDRKTIAQ 670 680 690 700 710 720 AKKISNPGCY ATAAQVAIAP LKEYISGTPS IFGVSGYSGA GTKPSPKNDV NLLSNNLIPY 730 740 750 760 770 780 SLTDHVHEKE ISSQLGLQVA FTPHVAQWFQ GITHTINIPI KKGSLTSREI RNIYQDRYQG 790 800 810 820 830 840 EKLITISGEA PLVKDISGKH GVVVGGFAVN SNEDRVVIVA TIDNLLKGAA TQCLQNINLS 850 QEFGEYDGIP TESLIRG

References

[1]	"Cloning, analysis and one-step disruption of the ARG5,6 gene of Candida albicans." Negredo A., Monteoliva L., Gil C., Pla J., Nombela C. Microbiology 143:297-302(1997) [PubMed: 9043106] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 64385 / 1001.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X98880 Genomic DNA. Translation: CAA67383.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.1.38. 1124. 2.7.2.8. 1124.
Family and domain databases
InterPro	IPR004662. AcgluKinase. IPR000706. AGPR_act_site. IPR001048. Asp/Glu/Uridylate_kinase. IPR006855. DUF619. IPR011241. NAGK_NAGSA. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_C. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. PF04768. DUF619. 1 hit. PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
PIRSF	PIRSF036440. ARG5-6. 1 hit.
ProDom	PD003765. AGPR_act_site. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00761. argB. 1 hit. TIGR01850. argC. 1 hit.
PROSITE	PS01224. ARGC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARG56_CANAL

Accession

Primary (citable) accession number: P78586

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)