Q65G67 (ASSY_BACLD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 54.
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 | Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 279010 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 403 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 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 |
| 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 |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 403 | 403 | Argininosuccinate synthase HAMAP MF_00005 | PRO_0000148570 | |||||
Regions | |||||||||
| Nucleotide binding | 10 – 18 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 87 | 1 | Citrulline By similarity | ||||||
| Binding site | 117 | 1 | ATP; via amide nitrogen By similarity | ||||||
| Binding site | 119 | 1 | Aspartate By similarity | ||||||
| Binding site | 123 | 1 | Aspartate By similarity | ||||||
| Binding site | 123 | 1 | Citrulline By similarity | ||||||
| Binding site | 124 | 1 | Aspartate By similarity | ||||||
| Binding site | 127 | 1 | Citrulline By similarity | ||||||
| Binding site | 175 | 1 | Citrulline By similarity | ||||||
| Binding site | 184 | 1 | Citrulline By similarity | ||||||
| Binding site | 260 | 1 | Citrulline By similarity | ||||||
| Binding site | 272 | 1 | Citrulline By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
| [2] | "Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. Berka R.M.Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017333 Genomic DNA. Translation: AAU41947.1. CP000002 Genomic DNA. Translation: AAU24589.1. |
| RefSeq | YP_080227.1. NC_006270.3. YP_092640.1. NC_006322.1. |
3D structure databases | |
| ProteinModelPortal | Q65G67. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q65G67. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000057257; EBBACP00000055788; EBBACG00000057248. EBBACT00000061828; EBBACP00000060261; EBBACG00000061819. |
| GeneID | 3028521. 3098708. |
| GenomeReviews | Gene locus BLi03084 in contig AE017333_GR. Gene locus BL00417 in contig CP000002_GR. |
| KEGG | bld:BLi03084. bli:BL00417. |
| NMPDR | fig|279010.5.peg.3445. |
| PATRIC | 18951904. VBIBacLic203714_3152. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0137. |
| GeneTree | EBGT00050000002857. |
| HOGENOM | HBG335267. |
| OMA | LATYDTG. |
| PhylomeDB | Q65G67. |
| ProtClustDB | PRK00509. |
Enzyme and pathway databases | |
| BioCyc | BLIC279010-1:BLI03084-MONOMER. BLIC279010:BL00417-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_BACLD | ||||||||
| Accession | Primary (citable) accession number: Q65G67 Secondary accession number(s): Q62RM1 | ||||||||
| 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