Reviewed,
UniProtKB/Swiss-Prot Q98G36 (ARLY1_RHILO)
Last modified
November 3, 2009.
Version 55.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Argininosuccinate lyase 1 Short name=ASAL 1 EC=4.3.2.1 Alternative name(s): Arginosuccinase 1 | ||||
| Gene names |
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| Organism | Rhizobium loti (Mesorhizobium loti) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 381 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium |
Protein attributes
| Sequence length | 466 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. HAMAP MF_00006 |
| Pathway | Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. HAMAP MF_00006 |
| Subcellular location | Cytoplasm Probable. |
| Sequence similarities | Belongs to the lyase 1 family. Argininosuccinate lyase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | arginine biosynthetic process via ornithine Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | argininosuccinate lyase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 466 | 466 | Argininosuccinate lyase 1 HAMAP MF_00006 | PRO_0000137810 | |||
Sequences
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References
| [1] | "Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti." Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. Tabata S.DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MAFF303099. |
Cross-references
Sequence databases | |
|---|---|
| BA000012 Genomic DNA. Translation: BAB50380.1. | |
| RefSeq | NP_104594.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DCN based on UniProtKB P24058. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1227255. |
| GenomeReviews | Gene locus mlr3506 in contig BA000012_GR. |
| KEGG | mlo:mlr3506. |
| NMPDR | fig|266835.1.peg.2698. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q98G36. |
| OMA | MAEDLIF. |
Enzyme and pathway databases | |
| BRENDA | 4.3.2.1. 3315. |
Family and domain databases | |
| HAMAP | MF_00006. [Tree] |
| InterPro | IPR009049. Argininosuccinate_lyase. IPR003031. D_crystallin. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. [Graphical view] |
| PANTHER | PTHR11444:SF3. argH. 1 hit. |
| Pfam | PF00206. Lyase_1. 1 hit. [Graphical view] |
| PRINTS | PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE. |
| TIGRFAMs | TIGR00838. argH. 1 hit. |
| PROSITE | PS00163. FUMARATE_LYASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARLY1_RHILO | ||||||||
| Accession | Primary (citable) accession number: Q98G36 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


