Q9X2A4 (ARGB_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylglutamate kinase
EC=2.7.2.8

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

Gene names

Name:	argB
Ordered Locus Names:	TM_1784

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. HAMAP MF_00082_B
Enzyme regulation	Allosterically inhibited by arginine. HAMAP MF_00082_B
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP MF_00082_B
Subunit structure	Homohexamer. Ref.3
Subcellular location	Cytoplasm By similarity HAMAP MF_00082_B.
Sequence similarities	Belongs to the acetylglutamate kinase family.
Biophysicochemical properties	Temperature dependence: Active from 25 to 80 degrees Celsius. HAMAP MF_00082_B
Mass spectrometry	Molecular mass is 30341 Da from positions 1 - 282. Determined by MALDI. Ref.2 Molecular mass is 30352 Da from positions 1 - 282. Determined by ESI. Ref.3

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW proline biosynthetic process Inferred from electronic annotation. Source: InterPro
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 glutamate 5-kinase 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 – 282

282

Acetylglutamate kinase HAMAP MF_00082_B

PRO_0000112678

Regions

Region

62 – 63

2

Substrate binding By similarity

Region

266 – 269

4

Allosteric inhibitor binding HAMAP MF_00082_B

Sites

Binding site

84

1

Substrate By similarity

Binding site

178

1

Substrate

Binding site

196

1

Allosteric inhibitor

Binding site

214

1

Allosteric inhibitor

Site

27

1

Transition state stabilizer By similarity

Site

237

1

Transition state stabilizer By similarity

Secondary structure

1

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282

Helix Strand Turn

Details...

Helix

2 – 19

18

Beta strand

23 – 27

5

Turn

32 – 34

3

Helix

36 – 51

16

Beta strand

55 – 59

5

Helix

65 – 72

8

Helix

88 – 98

11

Helix

102 – 111

10

Helix

124 – 126

3

Beta strand

127 – 130

4

Beta strand

145 – 148

4

Helix

151 – 158

8

Beta strand

162 – 165

4

Helix

181 – 192

12

Beta strand

195 – 200

6

Helix

218 – 225

8

Helix

235 – 245

11

Beta strand

252 – 255

4

Helix

262 – 267

6

Sequences

	Sequence		Length	Mass (Da)
	Q9X2A4 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: A140CE3899BFA40A	FASTA	282	30,345
	10 20 30 40 50 60 MRIDTVNVLL EALPYIKEFY GKTFVIKFGG SAMKQENAKK AFIQDIILLK YTGIKPIIVH 70 80 90 100 110 120 GGGPAISQMM KDLGIEPVFK NGHRVTDEKT MEIVEMVLVG KINKEIVMNL NLHGGRAVGI 130 140 150 160 170 180 CGKDSKLIVA EKETKHGDIG YVGKVKKVNP EILHALIEND YIPVIAPVGI GEDGHSYNIN 190 200 210 220 230 240 ADTAAAEIAK SLMAEKLILL TDVDGVLKDG KLISTLTPDE AEELIRDGTV TGGMIPKVEC 250 260 270 280 AVSAVRGGVG AVHIINGGLE HAILLEIFSR KGIGTMIKEL EG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Arginine biosynthesis in Thermotoga maritima: characterization of the arginine-sensitive N-acetyl-L-glutamate kinase." Fernandez-Murga M.L., Gil-Ortiz F., Llacer J.L., Rubio V. J. Bacteriol. 186:6142-6149(2004) [PubMed: 15342584] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-35, CHARACTERIZATION, MASS SPECTROMETRY.
[3]	"Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa." Ramon-Maiques S., Fernandez-Murga M.L., Gil-Ortiz F., Vagin A., Fita I., Rubio V. J. Mol. Biol. 356:695-713(2006) [PubMed: 16376937] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ARGININE, MASS SPECTROMETRY, ALLOSTERIC INHIBITION BY ARGININE, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD36847.1.

PIR

C72211.

RefSeq

NP_229581.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BTY	X-ray	2.75	A/B/C	1-282	[»]

ProteinModelPortal

Q9X2A4.

SMR

Q9X2A4. Positions 1-282.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

897763.

GenomeReviews

Gene locus TM_1784 in contig AE000512_GR.

KEGG

tma:TM1784.

NMPDR

fig|243274.1.peg.1765.

PATRIC

23938553. VBITheMar51294_1804.

TIGR

TM_1784.

Phylogenomic databases

HOGENOM

HBG497643.

OMA

GGNAMID.

PhylomeDB

Q9X2A4.

ProtClustDB

PRK00942.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1784-MONOMER.

BRENDA

2.7.2.8. 6331.

Family and domain databases

HAMAP

MF_00082_B. ArgB_B.
[Tree]

InterPro

IPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_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.

PRINTS

PR00474. GLU5KINASE.

SUPFAM

SSF53633. Aa_kinase. 1 hit.

TIGRFAMs

TIGR00761. ArgB. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ARGB_THEMA

Accession

Primary (citable) accession number: Q9X2A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program