A5F0H0 (A5F0H0_VIBC3) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 43.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417 Short name=ADC HAMAP-Rule MF_01417 EC=4.1.1.19 HAMAP-Rule MF_01417 | ||||
| Gene names |
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| Organism | Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 345073 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › ![]() |
Protein attributes
| Sequence length | 661 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP-Rule MF_01417 |
| Catalytic activity | L-arginine = agmatine + CO2. SAAS SAAS002985 RuleBase RU003740 HAMAP-Rule MF_01417 |
| Cofactor | Magnesium By similarity. SAAS SAAS002985 RuleBase RU003740 HAMAP-Rule MF_01417 Pyridoxal phosphate By similarity. SAAS SAAS002985 HAMAP-Rule MF_01417 |
| Pathway | Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP-Rule MF_01417 |
| Sequence similarities | Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. HAMAP-Rule MF_01417 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Polyamine biosynthesis HAMAP-Rule MF_01417 Spermidine biosynthesis SAAS SAAS002985 RuleBase RU003740 HAMAP-Rule MF_01417 |
| Ligand | Magnesium SAAS SAAS002985 HAMAP-Rule MF_01417 Metal-binding HAMAP-Rule MF_01417 Pyridoxal phosphate SAAS SAAS002985 HAMAP-Rule MF_01417 |
| Molecular function | Decarboxylase SAAS SAAS002985 RuleBase RU003740 HAMAP-Rule MF_01417 Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | arginine catabolic process Inferred from electronic annotation. Source: InterPro spermidine biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Molecular_function | arginine decarboxylase activity Inferred from electronic annotation. Source: HAMAP metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Region | 311 – 321 | 11 | Substrate-binding By similarity HAMAP-Rule MF_01417 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 126 | 1 | N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01417 | ||||||
Sequences
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References
| [1] | Heidelberg J. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39541 / Ogawa 395 / O395 [TIGR]. |
| [2] | "A recalibrated molecular clock and independent origins for the cholera pandemic clones." Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L. PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39541 / Ogawa 395 / O395 [Nankai/TEDA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000626 Genomic DNA. Translation: ABQ19043.1. CP001236 Genomic DNA. Translation: ACP11672.1. |
| RefSeq | YP_001215260.1. NC_009456.1. YP_002821908.1. NC_012583.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 345073.VC0395_0419. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABQ19043; ABQ19043; VC0395_0419. ACP11672; ACP11672; VC395_A0839. |
| GeneID | 5134840. 7777902. |
| KEGG | vco:VC0395_0419. vcr:VC395_A0839. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1166. |
| HOGENOM | HOG000029191. |
| KO | K01585. |
| OMA | MIHFHIG. |
| ProtClustDB | PRK05354. |
Enzyme and pathway databases | |
| UniPathway | UPA00186; UER00284. |
Family and domain databases | |
| Gene3D | 2.40.37.10. 2 hits. |
| HAMAP | MF_01417. SpeA. |
| InterPro | IPR009006. Ala_racemase/Decarboxylase_C. IPR002985. Arg_decrbxlase. IPR022643. De-COase2_C. IPR022644. De-COase2_N. IPR000183. Orn/DAP/Arg_de-COase. [Graphical view] |
| PANTHER | PTHR11482:SF3. PTHR11482:SF3. 1 hit. |
| Pfam | PF02784. Orn_Arg_deC_N. 1 hit. PF00278. Orn_DAP_Arg_deC. 1 hit. [Graphical view] |
| PIRSF | PIRSF001336. Arg_decrbxlase. 1 hit. |
| PRINTS | PR01180. ARGDCRBXLASE. PR01179. ODADCRBXLASE. |
| TIGRFAMs | TIGR01273. speA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | A5F0H0_VIBC3 | ||||||||
| Accession | Primary (citable) accession number: A5F0H0 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
