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Protein

Acetylglutamate kinase

Gene

argB

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate.1 Publication

Enzyme regulationi

Allosterically inhibited by arginine.1 Publication

Temperature dependencei

Active from 25 to 80 degrees Celsius.1 Publication

Pathwayi: L-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Arginine biosynthesis bifunctional protein ArgJ (argJ), Arginine biosynthesis bifunctional protein ArgJ (argJ)
  2. Acetylglutamate kinase (argB), Acetylglutamate kinase (Tmari_1793)
  3. N-acetyl-gamma-glutamyl-phosphate reductase (argC), N-acetyl-gamma-glutamyl-phosphate reductase (argC)
  4. Acetylornithine aminotransferase (argD), Acetylornithine aminotransferase (argD)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei27 – 271Transition state stabilizerBy similarity
Binding sitei84 – 841SubstrateBy similarity
Binding sitei178 – 1781Substrate1 Publication
Binding sitei196 – 1961Allosteric inhibitor
Binding sitei214 – 2141Allosteric inhibitor
Sitei237 – 2371Transition state stabilizerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.2.8. 6331.
UniPathwayiUPA00068; UER00107.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylglutamate kinase (EC:2.7.2.8)
Alternative name(s):
N-acetyl-L-glutamate 5-phosphotransferase
NAG kinase
Short name:
AGK
Gene namesi
Name:argB
Ordered Locus Names:TM_1784
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Acetylglutamate kinasePRO_0000112678Add
BLAST

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

STRINGi243274.TM1784.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1918Combined sources
Beta strandi23 – 286Combined sources
Helixi31 – 344Combined sources
Helixi36 – 5116Combined sources
Beta strandi55 – 606Combined sources
Helixi64 – 729Combined sources
Beta strandi79 – 846Combined sources
Helixi88 – 10013Combined sources
Helixi102 – 11110Combined sources
Turni112 – 1143Combined sources
Beta strandi117 – 1215Combined sources
Helixi124 – 1263Combined sources
Beta strandi127 – 1326Combined sources
Beta strandi140 – 1489Combined sources
Helixi151 – 1588Combined sources
Beta strandi162 – 1709Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi176 – 1783Combined sources
Helixi181 – 19212Combined sources
Beta strandi195 – 20511Combined sources
Helixi218 – 2258Combined sources
Turni226 – 2283Combined sources
Helixi234 – 24613Combined sources
Beta strandi252 – 2565Combined sources
Helixi262 – 2676Combined sources
Beta strandi268 – 2714Combined sources
Beta strandi273 – 2775Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BTYX-ray2.75A/B/C1-282[»]
ProteinModelPortaliQ9X2A4.
SMRiQ9X2A4. Positions 1-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X2A4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 632Substrate bindingBy similarity
Regioni266 – 2694Allosteric inhibitor binding

Sequence similaritiesi

Belongs to the acetylglutamate kinase family.Curated

Phylogenomic databases

eggNOGiENOG4105CAS. Bacteria.
COG0548. LUCA.
InParanoidiQ9X2A4.
KOiK00930.
OMAiPKTECCI.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_00082_A. ArgB_A. 1 hit.
MF_00082_B. ArgB_B. 1 hit.
InterProiIPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000728. NAGK. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9X2A4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIDTVNVLL EALPYIKEFY GKTFVIKFGG SAMKQENAKK AFIQDIILLK
60 70 80 90 100
YTGIKPIIVH GGGPAISQMM KDLGIEPVFK NGHRVTDEKT MEIVEMVLVG
110 120 130 140 150
KINKEIVMNL NLHGGRAVGI CGKDSKLIVA EKETKHGDIG YVGKVKKVNP
160 170 180 190 200
EILHALIEND YIPVIAPVGI GEDGHSYNIN ADTAAAEIAK SLMAEKLILL
210 220 230 240 250
TDVDGVLKDG KLISTLTPDE AEELIRDGTV TGGMIPKVEC AVSAVRGGVG
260 270 280
AVHIINGGLE HAILLEIFSR KGIGTMIKEL EG
Length:282
Mass (Da):30,345
Last modified:November 1, 1999 - v1
Checksum:iA140CE3899BFA40A
GO

Mass spectrometryi

Molecular mass is 30341 Da from positions 1 - 282. Determined by MALDI. 1 Publication
Molecular mass is 30352 Da from positions 1 - 282. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36847.1.
PIRiC72211.
RefSeqiNP_229581.1. NC_000853.1.
WP_004082330.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36847; AAD36847; TM_1784.
GeneIDi897763.
KEGGitma:TM1784.
tmi:THEMA_05280.
tmw:THMA_1828.
PATRICi23938553. VBITheMar51294_1804.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36847.1.
PIRiC72211.
RefSeqiNP_229581.1. NC_000853.1.
WP_004082330.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BTYX-ray2.75A/B/C1-282[»]
ProteinModelPortaliQ9X2A4.
SMRiQ9X2A4. Positions 1-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1784.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36847; AAD36847; TM_1784.
GeneIDi897763.
KEGGitma:TM1784.
tmi:THEMA_05280.
tmw:THMA_1828.
PATRICi23938553. VBITheMar51294_1804.

Phylogenomic databases

eggNOGiENOG4105CAS. Bacteria.
COG0548. LUCA.
InParanoidiQ9X2A4.
KOiK00930.
OMAiPKTECCI.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00107.
BRENDAi2.7.2.8. 6331.

Miscellaneous databases

EvolutionaryTraceiQ9X2A4.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_00082_A. ArgB_A. 1 hit.
MF_00082_B. ArgB_B. 1 hit.
InterProiIPR004662. AcgluKinase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000728. NAGK. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiARGB_THEMA
AccessioniPrimary (citable) accession number: Q9X2A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: September 7, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.