P77973 (ASSY_SYNY3) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 83.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Argininosuccinate synthase EC=6.3.4.5 Alternative name(s): Citrulline--aspartate ligase | ||||
| Gene names |
| ||||
| Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) | ||||
| Taxonomic identifier | 1111708 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Chroococcales › Synechocystis |
Protein attributes
| Sequence length | 400 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP MF_00005 |
| Pathway | Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP MF_00005 |
| Subunit structure | Homotetramer By similarity. HAMAP MF_00005 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00005. |
| Sequence similarities | Belongs to the argininosuccinate synthase family. Type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome Reference proteome |
| 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 | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW argininosuccinate synthase activityInferred from electronic annotation. Source: EC protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| trxA | P52231 | 2 | EBI-862317,EBI-862916 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 400 | 400 | Argininosuccinate synthase HAMAP MF_00005 | PRO_0000148655 | |||||
Regions | |||||||||
| Nucleotide binding | 10 – 18 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 38 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 89 | 1 | Citrulline By similarity | ||||||
| Binding site | 119 | 1 | ATP; via amide nitrogen By similarity | ||||||
| Binding site | 121 | 1 | Aspartate By similarity | ||||||
| Binding site | 125 | 1 | Aspartate By similarity | ||||||
| Binding site | 125 | 1 | Citrulline By similarity | ||||||
| Binding site | 126 | 1 | Aspartate By similarity | ||||||
| Binding site | 129 | 1 | Citrulline By similarity | ||||||
| Binding site | 177 | 1 | Citrulline By similarity | ||||||
| Binding site | 186 | 1 | Citrulline By similarity | ||||||
| Binding site | 262 | 1 | Citrulline By similarity | ||||||
| Binding site | 274 | 1 | Citrulline By similarity | ||||||
Sequences
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References
| [1] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000022 Genomic DNA. Translation: BAA18841.1. |
| PIR | S76929. |
| RefSeq | NP_443029.1. NC_000911.1. |
3D structure databases | |
| ProteinModelPortal | P77973. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P77973. 7 interactions. |
| STRING | P77973. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 951914. |
| GenomeReviews | Gene locus slr0585 in contig BA000022_GR. |
| KEGG | syn:slr0585. |
| NMPDR | fig|1148.1.peg.3130. |
| PATRIC | 23843914. VBISynSp132158_3487. |
Phylogenomic databases | |
| eggNOG | COG0137. |
| HOGENOM | HBG335267. |
| OMA | DIAHENE. |
| PhylomeDB | P77973. |
| ProtClustDB | PRK00509. |
Enzyme and pathway databases | |
| BioCyc | SSP1148:SLR0585-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00005. Arg_succ_synth_type1. [Tree] |
| InterPro | IPR001518. Arginosuc_synth. IPR018223. Arginosuc_synth_CS. IPR023434. Arginosuc_synth_type_1_subfam. IPR024074. AS_cat/multimer_dom_body. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:3.90.1260.10. G3DSA:3.90.1260.10. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| KO | K01940. |
| PANTHER | PTHR11587. Arginosuc_synth. 1 hit. |
| Pfam | PF00764. Arginosuc_synth. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00032. ArgG. 1 hit. |
| PROSITE | PS00564. ARGININOSUCCIN_SYN_1. 1 hit. PS00565. ARGININOSUCCIN_SYN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ASSY_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: P77973 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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