O59397 (ARGC_PYRHO) Reviewed, UniProtKB/Swiss-Prot

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.-
EC=1.2.1.38

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:	PH1720

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in both the arginine and lysine biosynthetic pathways By similarity. HAMAP MF_00150
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 HAMAP MF_00150.
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: UniProtKB-KW lysine biosynthetic process 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: EC NAD 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 – 330	330	N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase HAMAP MF_00150		PRO_0000112495
Sites
	Active site	142	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O59397 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: F6B7AE6F04962F3C	FASTA	330	37,168
	10 20 30 40 50 60 MIKVAIVGGS GYIGGELIRL LAMHPEVEIV AVTSREYAGK KVHKVHPNLR GLNLRFTSDY 70 80 90 100 110 120 NFDADVIFLA VPHGVSMKLI NEFLGSAKII DLSADFRVRK ELYEKYYGKH ERPELIEDFV 130 140 150 160 170 180 YGLPEIHRKE IKKAELVANP GCNATAVILA LYPFKDLTKE VLVDLKVSSS AGGRRENLPS 190 200 210 220 230 240 IHPERSNVVR VYKPYHHRHE AEVLQETGVR AMFTVHSVDI VRGLLATIYF TFEGNEKDLL 250 260 270 280 290 300 KRMLIYKDEP FIRLVVDKGG LQRYPDPKYV LGSNFVDLGL AYDEENSRVI VFSALDNLIK 310 320 330 GGAGQAVQNM NIMFGLDETL GLGYYPLYPV

References

[1]

"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000001 Genomic DNA. Translation: BAA30834.1.
PIR	C71180.
RefSeq	NP_143561.1. NC_000961.1.
3D structure databases
ProteinModelPortal	O59397.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000000178; EBPYRP00000000178; EBPYRG00000000178.
GeneID	1442565.
GenomeReviews	Gene locus PH1720 in contig BA000001_GR.
KEGG	pho:PH1720.
NMPDR	fig|70601.1.peg.1679.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000022773.
HOGENOM	HBG294213.
OMA	VYRYPEP.
PhylomeDB	O59397.
ProtClustDB	PRK00436.
Enzyme and pathway databases
BioCyc	PHOR70601:PH1720-MONOMER.
Family and domain databases
HAMAP	MF_00150. ArgC_type1. [Tree]
InterPro	IPR023013. AGPR_AS. IPR000706. AGPR_type-1. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_dimer_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00145.
Pfam	PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01850. ArgC. 1 hit.
PROSITE	PS01224. ARGC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGC_PYRHO

Accession

Primary (citable) accession number: O59397

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program