Q8PZL8 (ARGJ_METMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 62.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Arginine biosynthesis bifunctional protein ArgJ Cleaved into the following 2 chains: | ||||
| Gene names |
| ||||
| Organism | Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 192952 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina |
Protein attributes
| Sequence length | 395 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate By similarity. HAMAP MF_01106 |
| Catalytic activity | N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. HAMAP MF_01106 Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01106 |
| Pathway | Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. HAMAP MF_01106 Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01106 |
| Subunit structure | Heterotetramer of two alpha and two beta chains By similarity. |
| Subcellular location | Cytoplasm Probable HAMAP MF_01106. |
| Miscellaneous | Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway. HAMAP MF_01106 |
| Sequence similarities | Belongs to the ArgJ family. |
| Sequence caution | The sequence AAM30170.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Acyltransferase Transferase |
| PTM | Autocatalytic cleavage |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: EC glutamate N-acetyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. Gottschalk G.J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE008384 Genomic DNA. Translation: AAM30170.1. Different initiation. |
| RefSeq | NP_632498.1. NC_003901.1. |
3D structure databases | |
| ProteinModelPortal | Q8PZL8. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | T05.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1478816. |
| GenomeReviews | Gene locus MM_0474 in contig AE008384_GR. |
| KEGG | mma:MM_0474. |
| NMPDR | fig|192952.1.peg.474. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG284202. |
| OMA | GRDPNWG. |
| PhylomeDB | Q8PZL8. |
| ProtClustDB | PRK05388. |
Enzyme and pathway databases | |
| BioCyc | MMAZ192952:MM0474-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01106. ArgJ. Divergent sequence. [Tree] |
| InterPro | IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view] |
| KO | K00620. |
| PANTHER | PTHR23100. ArgJ. 1 hit. |
| Pfam | PF01960. ArgJ. 1 hit. [Graphical view] |
| ProDom | PD004193. Arg_biosynth_ArgJ. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SUPFAM | SSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit. |
| TIGRFAMs | TIGR00120. ArgJ. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ARGJ_METMA | ||||||||
| Accession | Primary (citable) accession number: Q8PZL8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with