E7FCP8 · NAGS_DANRE
- ProteinN-acetylglutamate synthase, mitochondrial
- Genenags
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids527 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in the regulation of ureagenesis by producing the essential cofactor N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (cps1) activity.
Catalytic activity
- acetyl-CoA + L-glutamate = CoA + H+ + N-acetyl-L-glutamate
Activity regulation
Inhibited by L-arginine.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.22 mM | acetyl-CoA | |||||
1.13 mM | L-glutamate |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 386 | substrate | ||||
Sequence: K | ||||||
Binding site | 429 | substrate | ||||
Sequence: K | ||||||
Binding site | 459-464 | substrate | ||||
Sequence: RSRTTN |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | acetyl-CoA:L-glutamate N-acetyltransferase activity | |
Molecular Function | arginine binding | |
Molecular Function | methione N-acyltransferase activity | |
Biological Process | arginine biosynthetic process | |
Biological Process | glutamate metabolic process | |
Biological Process | urea cycle |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-acetylglutamate synthase, mitochondrial
- EC number
- Cleaved into 2 chains
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionE7FCP8
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-39 | Mitochondrion | ||||
Sequence: MAKVNSGSSGCRAMVMAGQFWTKPFALSSQRSGPHRRSA | ||||||
Chain | PRO_0000444987 | 40-527 | N-acetylglutamate synthase, mature form | |||
Sequence: AEVNRRMSSSRTAGHGSKTPLWSQQESYNHSSLGERSAWSNRTLIYRDVKAFLREIGGDPREARYWLTHFQRAGSTPAFAVLEVDPSVFDSHEMVQSLAFGLSFLQRMDMKLVVVMGLPAEITEDDHTRSATDSPLARTVMVKHCQALTEALQDNSANVMPFFSSEALLQLQDNPLDGSSSGPSVVVDSALLQWTLDCRVIPLVCPVGRDTTGRSSVLRSIQVTTAISQTLQPLKVIFLNSSGGIRNQNHKVLGLVSLPGDLPALSCAEWLNEVEQKRIGSIAELLNLLPVESSAVLTSANTLLTELFSHKGSGTLFKNGDPIRRYSSLEDIDVDRLLALINKSFEKNLREDYIASLEGRLHSVYLSEGYSAAAIITTEPVNSGTPYLDKFVVSSSKQGQGTGQILWECIRQDFSKLFWRSRTTNRINPWYFKHCDGSFVNGHWIVFWLGLSDIRESYELVEFAKSHPDSFCSLSTTETKPLQQHHGS | ||||||
Chain | PRO_0000444988 | 84-527 | N-acetylglutamate synthase, conserved domain form | |||
Sequence: IYRDVKAFLREIGGDPREARYWLTHFQRAGSTPAFAVLEVDPSVFDSHEMVQSLAFGLSFLQRMDMKLVVVMGLPAEITEDDHTRSATDSPLARTVMVKHCQALTEALQDNSANVMPFFSSEALLQLQDNPLDGSSSGPSVVVDSALLQWTLDCRVIPLVCPVGRDTTGRSSVLRSIQVTTAISQTLQPLKVIFLNSSGGIRNQNHKVLGLVSLPGDLPALSCAEWLNEVEQKRIGSIAELLNLLPVESSAVLTSANTLLTELFSHKGSGTLFKNGDPIRRYSSLEDIDVDRLLALINKSFEKNLREDYIASLEGRLHSVYLSEGYSAAAIITTEPVNSGTPYLDKFVVSSSKQGQGTGQILWECIRQDFSKLFWRSRTTNRINPWYFKHCDGSFVNGHWIVFWLGLSDIRESYELVEFAKSHPDSFCSLSTTETKPLQQHHGS |
Proteomic databases
Expression
Developmental stage
Detected in 32-cell embryos, probably due to perdurance of maternal transcripts. Has low expression at the 90% epiboly and tailbud stages (9-10 hours post-fertilization, hpf). Moderately expressed from 24 hpf onwards, and strongly expressed at the adult stage.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 28-65 | Disordered | ||||
Sequence: SSQRSGPHRRSAAEVNRRMSSSRTAGHGSKTPLWSQQE | ||||||
Region | 40-83 | May stabilize the oligomeric structure | ||||
Sequence: AEVNRRMSSSRTAGHGSKTPLWSQQESYNHSSLGERSAWSNRTL | ||||||
Region | 40-361 | Amino-acid kinase domain (AAK) | ||||
Sequence: AEVNRRMSSSRTAGHGSKTPLWSQQESYNHSSLGERSAWSNRTLIYRDVKAFLREIGGDPREARYWLTHFQRAGSTPAFAVLEVDPSVFDSHEMVQSLAFGLSFLQRMDMKLVVVMGLPAEITEDDHTRSATDSPLARTVMVKHCQALTEALQDNSANVMPFFSSEALLQLQDNPLDGSSSGPSVVVDSALLQWTLDCRVIPLVCPVGRDTTGRSSVLRSIQVTTAISQTLQPLKVIFLNSSGGIRNQNHKVLGLVSLPGDLPALSCAEWLNEVEQKRIGSIAELLNLLPVESSAVLTSANTLLTELFSHKGSGTLFKNGDP | ||||||
Compositional bias | 44-65 | Polar residues | ||||
Sequence: RRMSSSRTAGHGSKTPLWSQQE | ||||||
Domain | 360-511 | N-acetyltransferase | ||||
Sequence: DPIRRYSSLEDIDVDRLLALINKSFEKNLREDYIASLEGRLHSVYLSEGYSAAAIITTEPVNSGTPYLDKFVVSSSKQGQGTGQILWECIRQDFSKLFWRSRTTNRINPWYFKHCDGSFVNGHWIVFWLGLSDIRESYELVEFAKSHPDSFC |
Domain
The amino-acid kinase (AAK) domain mediates binding of L-arginine.
Sequence similarities
Belongs to the acetyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length527
- Mass (Da)58,407
- Last updated2011-03-08 v1
- Checksum657FE482B70566D3
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8M9PJE2 | A0A8M9PJE2_DANRE | nags | 526 | ||
A0A8M9P8E6 | A0A8M9P8E6_DANRE | nags | 527 | ||
A0A8M9PWK2 | A0A8M9PWK2_DANRE | nags | 526 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 44-65 | Polar residues | ||||
Sequence: RRMSSSRTAGHGSKTPLWSQQE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL935200 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |