Reviewed,
UniProtKB/Swiss-Prot Q8G5F2 (ASSY_BIFLO)
Last modified
February 9, 2010.
Version 45.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Argininosuccinate synthase EC=6.3.4.5 Alternative name(s): Citrulline--aspartate ligase | ||||
| Gene names |
| ||||
| Organism | Bifidobacterium longum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 216816 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium |
Protein attributes
| Sequence length | 412 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
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 Probable 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 |
| Gene Ontology (GO) | |
| Biological process | arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP argininosuccinate synthase activityInferred 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 – 412 | 412 | Argininosuccinate synthase HAMAP MF_00005 | PRO_0000148573 | |||||
Regions | |||||||||
| Nucleotide binding | 10 – 18 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| 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 | 261 | 1 | Citrulline By similarity | ||||||
| Binding site | 273 | 1 | Citrulline By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract." Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F. Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 2705. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014295 Genomic DNA. Translation: AAN24866.1. |
| RefSeq | NP_696230.1. |
3D structure databases | |
| SMR | Q8G5F2. Positions 6-396. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1022588. |
| GenomeReviews | Gene locus BL1058 in contig AE014295_GR. |
| KEGG | blo:BL1058. |
| NMPDR | fig|206672.1.peg.997. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG335267. |
| OMA | IAPVREW. |
| PhylomeDB | Q8G5F2. |
Enzyme and pathway databases | |
| BioCyc | BLON206672:BL1058-MONOMER. |
| BRENDA | 6.3.4.5. 39917. |
Family and domain databases | |
| HAMAP | MF_00005. Arg_succ_synth_type1. [Tree] |
| InterPro | IPR001518. Arginosuc_synth. IPR018223. Arginosuc_synth_CS. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| 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_BIFLO | ||||||||
| Accession | Primary (citable) accession number: Q8G5F2 | ||||||||
| Entry history |
| ||||||||
| 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


