UniProtKB - Q9X2A4 (ARGB_THEMA)
Protein
Acetylglutamate kinase
Gene
argB
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Functioni
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.UniRule annotation1 Publication
Catalytic activityi
- EC:2.7.2.8UniRule annotation1 Publication
Activity regulationi
Allosterically inhibited by arginine.1 Publication
Temperature dependencei
Active from 25 to 80 degrees Celsius.1 Publication
: L-arginine biosynthesis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.UniRule annotation1 PublicationProteins known to be involved in the 4 steps of the subpathway in this organism are:
- Arginine biosynthesis bifunctional protein ArgJ (argJ), Arginine biosynthesis bifunctional protein ArgJ (argJ)
- Acetylglutamate kinase (argB), Acetylglutamate kinase (argB)
- N-acetyl-gamma-glutamyl-phosphate reductase (argC), N-acetyl-gamma-glutamyl-phosphate reductase (argC)
- Acetylornithine aminotransferase (argD), Acetylornithine aminotransferase (argD)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 27 | Transition state stabilizerUniRule annotation | 1 | |
Binding sitei | 84 | SubstrateUniRule annotation | 1 | |
Binding sitei | 178 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 196 | L-arginine binding; allosteric inhibitorCombined sources1 Publication | 1 | |
Binding sitei | 214 | L-arginine binding; allosteric inhibitorCombined sources1 Publication | 1 | |
Sitei | 237 | Transition state stabilizerUniRule annotation | 1 |
GO - Molecular functioni
- acetylglutamate kinase activity Source: GO_Central
- arginine binding Source: GO_Central
- ATP binding Source: UniProtKB-UniRule
GO - Biological processi
- arginine biosynthetic process Source: GO_Central
- arginine biosynthetic process via ornithine Source: UniProtKB-UniRule
Keywordsi
Molecular function | Allosteric enzyme, Kinase, Transferase |
Biological process | Amino-acid biosynthesis, Arginine biosynthesis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.2.8, 6331 |
UniPathwayi | UPA00068;UER00107 |
Names & Taxonomyi
Protein namesi | Recommended name: Acetylglutamate kinaseUniRule annotation (EC:2.7.2.8UniRule annotation1 Publication)Alternative name(s): N-acetyl-L-glutamate 5-phosphotransferaseUniRule annotation NAG kinaseUniRule annotation Short name: NAGKUniRule annotation |
Gene namesi | Name:argBUniRule annotation Ordered Locus Names:TM_1784 |
Organismi | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
Taxonomic identifieri | 243274 [NCBI] |
Taxonomic lineagei | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000112678 | 1 – 282 | Acetylglutamate kinaseAdd BLAST | 282 |
Interactioni
Subunit structurei
Homohexamer.
1 PublicationProtein-protein interaction databases
STRINGi | 243274.THEMA_05280 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q9X2A4 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9X2A4 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 62 – 63 | Substrate bindingUniRule annotation | 2 | |
Regioni | 266 – 269 | L-arginine binding; allosteric inhibitorCombined sources1 Publication | 4 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0548, Bacteria |
InParanoidi | Q9X2A4 |
OMAi | GRVQHSI |
OrthoDBi | 901370at2 |
Family and domain databases
CDDi | cd04250, AAK_NAGK-C, 1 hit |
Gene3Di | 3.40.1160.10, 1 hit |
HAMAPi | MF_00082, ArgB, 1 hit |
InterProi | View protein in InterPro IPR036393, AceGlu_kinase-like_sf IPR004662, AcgluKinase_fam IPR037528, ArgB IPR001048, Asp/Glu/Uridylate_kinase IPR001057, Glu/AcGlu_kinase IPR041727, NAGK-C |
Pfami | View protein in Pfam PF00696, AA_kinase, 1 hit |
PIRSFi | PIRSF000728, NAGK, 1 hit |
PRINTSi | PR00474, GLU5KINASE |
SUPFAMi | SSF53633, SSF53633, 1 hit |
TIGRFAMsi | TIGR00761, argB, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9X2A4-1 [UniParc]FASTAAdd to basket
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
Mass spectrometryi
Molecular mass is 30341 Da. Determined by MALDI. 1 Publication
Molecular mass is 30352 Da. Determined by ESI. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000512 Genomic DNA Translation: AAD36847.1 |
PIRi | C72211 |
RefSeqi | NP_229581.1, NC_000853.1 WP_004082330.1, NZ_CP011107.1 |
Genome annotation databases
EnsemblBacteriai | AAD36847; AAD36847; TM_1784 |
KEGGi | tma:TM1784 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000512 Genomic DNA Translation: AAD36847.1 |
PIRi | C72211 |
RefSeqi | NP_229581.1, NC_000853.1 WP_004082330.1, NZ_CP011107.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2BTY | X-ray | 2.75 | A/B/C | 1-282 | [»] | |
SMRi | Q9X2A4 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 243274.THEMA_05280 |
Genome annotation databases
EnsemblBacteriai | AAD36847; AAD36847; TM_1784 |
KEGGi | tma:TM1784 |
Phylogenomic databases
eggNOGi | COG0548, Bacteria |
InParanoidi | Q9X2A4 |
OMAi | GRVQHSI |
OrthoDBi | 901370at2 |
Enzyme and pathway databases
UniPathwayi | UPA00068;UER00107 |
BRENDAi | 2.7.2.8, 6331 |
Miscellaneous databases
EvolutionaryTracei | Q9X2A4 |
Family and domain databases
CDDi | cd04250, AAK_NAGK-C, 1 hit |
Gene3Di | 3.40.1160.10, 1 hit |
HAMAPi | MF_00082, ArgB, 1 hit |
InterProi | View protein in InterPro IPR036393, AceGlu_kinase-like_sf IPR004662, AcgluKinase_fam IPR037528, ArgB IPR001048, Asp/Glu/Uridylate_kinase IPR001057, Glu/AcGlu_kinase IPR041727, NAGK-C |
Pfami | View protein in Pfam PF00696, AA_kinase, 1 hit |
PIRSFi | PIRSF000728, NAGK, 1 hit |
PRINTSi | PR00474, GLU5KINASE |
SUPFAMi | SSF53633, SSF53633, 1 hit |
TIGRFAMsi | TIGR00761, argB, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ARGB_THEMA | |
Accessioni | Q9X2A4Primary (citable) accession number: Q9X2A4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | November 1, 1999 | |
Last modified: | April 7, 2021 | |
This is version 147 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families