Reviewed, UniProtKB/Swiss-Prot Q9YBY8 (ARGC_AERPE)

Names and origin

Protein names

Recommended name:
    N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase
      Short name=AGPR
    EC=1.2.1.38
    EC=1.2.1.-
Alternative name(s):
    N-acetyl-glutamate semialdehyde/N-acetyl-aminoadipate semialdehyde dehydrogenase
      Short name=NAGSA dehydrogenase

Gene names

Name:	argC
Synonyms:	lysY
Ordered Locus Names:	APE_1462

Organism

Aeropyrum pernix [Complete proteome] [HAMAP]

Taxonomic identifier

56636 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Involved in both the arginine and lysine biosynthetic pathways By similarity.
Catalytic activity	N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. HAMAP MF_00150 N(2)-acetyl-L-aminoadipate-semialdehyde + NADP+ + phosphate = N(2)-acetyl-L-gamma-aminoadipyl phosphate + NADPH. HAMAP MF_00150
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. HAMAP MF_00150 Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 3/5. HAMAP MF_00150
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP lysine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: HAMAP NAD or NADH binding Inferred from electronic annotation. Source: InterPro 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
	Chain	1 – 355	355	N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase HAMAP MF_00150		PRO_0000112482
Sites
	Active site	153	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9YBY8-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 94AFF4461A267A7A	FASTA	355	38,011
	10 20 30 40 50 60 MARAVRAGIL GASGMTGGEL LRILASHPGV EVEWATSREY AGKPVHTAHP HLRGFYTGLK 70 80 90 100 110 120 YTSIDKIDIG EVDVVFNALP HGVGASIVAE AYENGVRVVD LSADYRLRDQ SLYPKLYGFK 130 140 150 160 170 180 HPRPDLLEEA IYALPEIYGE KLRGARLAAV PGCNATAAIL AAAPLVASKI IDMDVGIIVD 190 200 210 220 230 240 VKAASSEAGS KPSRHSIHPL REGSARPYTP WGHRHAAEAV QVLRDLVGRG IRLSLVPHAV 250 260 270 280 290 300 SMTRGVLASA HALLRDNIGF SEAVRAYASF YKDSQIVRVK PMAPGLPVDP PDVKNVIGSM 310 320 330 340 350 FAEVGFAVEE ESGRITGFAA IDNLVRGAAG QAVYAMNAML GFDEWEGLRS PPLRP

References

[1]

"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000002 Genomic DNA. Translation: BAA80460.1.
PIR	F72625.
RefSeq	NP_147960.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1446031.
GenomeReviews	Gene locus APE_1462 in contig BA000002_GR.
KEGG	ape:APE_1462.
NMPDR	fig|272557.1.peg.1068.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9YBY8.
OMA	Q9YBY8. GCNATAT.
Enzyme and pathway databases
BRENDA	1.2.1.38. 256344.
Family and domain databases
HAMAP	MF_00150. [Tree]
InterPro	IPR000706. AGPR_act_site. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_C. [Graphical view]
Pfam	PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
ProDom	PD003765. AGPR_act_site. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01850. argC. 1 hit.
PROSITE	PS01224. ARGC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGC_AERPE

Accession

Primary (citable) accession number: Q9YBY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)