Q7VTJ9 (ASSY_BORPE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 55.
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: Argininosuccinate synthase EC=6.3.4.5 Alternative name(s): Citrulline--aspartate ligase | ||||
| Gene names |
| ||||
| Organism | Bordetella pertussis | ||||
| Taxonomic identifier | 520 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 445 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_00581 |
| Pathway | Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP MF_00581 |
| Subunit structure | Homotetramer By similarity. HAMAP MF_00581 |
| Subcellular location | Cytoplasm Probable HAMAP MF_00581. |
| Sequence similarities | Belongs to the argininosuccinate synthase family. Type 2 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 homodimerization activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 445 | 445 | Argininosuccinate synthase HAMAP MF_00581 | PRO_0000148692 | |||||
Regions | |||||||||
| Nucleotide binding | 17 – 25 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 43 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 99 | 1 | Citrulline By similarity | ||||||
| Binding site | 129 | 1 | ATP; via amide nitrogen By similarity | ||||||
| Binding site | 131 | 1 | Aspartate By similarity | ||||||
| Binding site | 131 | 1 | ATP By similarity | ||||||
| Binding site | 135 | 1 | Aspartate By similarity | ||||||
| Binding site | 135 | 1 | Citrulline By similarity | ||||||
| Binding site | 136 | 1 | Aspartate By similarity | ||||||
| Binding site | 136 | 1 | ATP By similarity | ||||||
| Binding site | 139 | 1 | Citrulline By similarity | ||||||
| Binding site | 192 | 1 | Citrulline By similarity | ||||||
| Binding site | 194 | 1 | ATP By similarity | ||||||
| Binding site | 201 | 1 | Citrulline By similarity | ||||||
| Binding site | 203 | 1 | Citrulline By similarity | ||||||
| Binding site | 280 | 1 | Citrulline By similarity | ||||||
Sequences
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References
| [1] | "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. Maskell D.J.Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX640421 Genomic DNA. Translation: CAE43796.1. |
| RefSeq | NP_882052.1. NC_002929.2. |
3D structure databases | |
| ProteinModelPortal | Q7VTJ9. |
| SMR | Q7VTJ9. Positions 2-442. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2664934. |
| GenomeReviews | Gene locus BP3537 in contig BX470248_GR. |
| KEGG | bpe:BP3537. |
| NMPDR | fig|257313.1.peg.3122. |
| PATRIC | 21160728. VBIBorPer7866_3829. |
Phylogenomic databases | |
| HOGENOM | HBG289560. |
| OMA | GGRKEMS. |
| PhylomeDB | Q7VTJ9. |
| ProtClustDB | PRK05370. |
Enzyme and pathway databases | |
| BioCyc | BPER257313:BP3537-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00581. Arg_succ_synth_type2. [Tree] |
| InterPro | IPR023437. Arg_succ_synth_type2_subfam. IPR001518. Arginosuc_synth. IPR018223. Arginosuc_synth_CS. IPR024074. AS_cat/multimer_dom_body. IPR024073. AS_multimer_C_tail. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:1.10.287.400. G3DSA:1.10.287.400. 1 hit. 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_BORPE | ||||||||
| Accession | Primary (citable) accession number: Q7VTJ9 | ||||||||
| Entry history |
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| 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