O59398 (ARGB_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylglutamate/acetylaminoadipate kinase
EC=2.7.2.-
EC=2.7.2.8

Alternative name(s):
N-acetyl-L-glutamate/N-acetyl-L-aminoadipate 5-phosphotransferase
NAG kinase
Short name=AGK

Gene names

Name:	argB
Synonyms:	lysZ
Ordered Locus Names:	PH1718

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	249 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_00082_A
Catalytic activity	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. HAMAP MF_00082_A ATP + N-acetyl-L-aminoadipate = ADP + N-acetyl-L-aminoadipate 5-phosphate. HAMAP MF_00082_A
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP MF_00082_A Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 2/5. HAMAP MF_00082_A
Subcellular location	Cytoplasm By similarity HAMAP MF_00082_A.
Sequence similarities	Belongs to the acetylglutamate kinase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
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	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetylglutamate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 249	249	Acetylglutamate/acetylaminoadipate kinase HAMAP MF_00082_A		PRO_0000112702
Regions
	Region	37 – 38	2	Substrate binding By similarity
Sites
	Binding site	64	1	Substrate By similarity
	Binding site	166	1	Substrate By similarity
	Site	10	1	Transition state stabilizer By similarity
	Site	222	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	O59398 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 6C1209090EFC8305	FASTA	249	27,847
	10 20 30 40 50 60 MRWVSMRVIK VGGSVLENLE KVFKPEIFRD AVVVHGGSRY VDELAKKLGL NVEKLTSPSG 70 80 90 100 110 120 VTFRRTTRKV LDVYIAAVMK ANRELVSFLR RQGIEAIGVS GVKEVIIGRR KKLIKAVING 130 140 150 160 170 180 KIMAIRDDYS GIIKEVNVEM IRNYMKVGVP VIAPIAYDPV ENVPLNVDGD KVAYHVALAL 190 200 210 220 230 240 KSRELYFLSD TAFLINGEVI DKIPRNRIEE YFPYSSGGMR KKLLMAKKAI ESGVERVIIE GLNGRTVIS

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: BAA30832.1.
PIR	A71180.
RefSeq	NP_143560.1. NC_000961.1.
3D structure databases
ProteinModelPortal	O59398.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000000346; EBPYRP00000000346; EBPYRG00000000346.
GeneID	1442564.
GenomeReviews	Gene locus PH1718 in contig BA000001_GR.
KEGG	pho:PH1718.
NMPDR	fig|70601.1.peg.1678.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000022350.
HOGENOM	HBG497643.
PhylomeDB	O59398.
ProtClustDB	PRK14058.
Enzyme and pathway databases
BioCyc	PHOR70601:PH1718-MONOMER.
Family and domain databases
HAMAP	MF_00082_A. ArgB_A. [Tree]
InterPro	IPR004662. AcgluKinase. IPR001048. Asp/Glu/Uridylate_kinase. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
KO	K00930.
Pfam	PF00696. AA_kinase. 1 hit. [Graphical view]
PIRSF	PIRSF000728. NAGK. 1 hit.
SUPFAM	SSF53633. Aa_kinase. 1 hit.
TIGRFAMs	TIGR00761. ArgB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGB_PYRHO

Accession

Primary (citable) accession number: O59398

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program