Reviewed,
UniProtKB/Swiss-Prot Q8XCX9 (SPEA_ECO57)
Last modified
November 3, 2009.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Biosynthetic arginine decarboxylase Short name=ADC EC=4.1.1.19 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 658 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the biosynthesis of agmatine from arginine By similarity. |
| Catalytic activity | L-arginine = agmatine + CO2. HAMAP MF_01417 |
| Cofactor | Magnesium By similarity. Pyridoxal phosphate By similarity. |
| Pathway | Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP MF_01417 |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Periplasm By similarity. |
| Sequence similarities | Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Polyamine biosynthesis Putrescine biosynthesis Spermidine biosynthesis |
| Cellular component | Periplasm |
| Ligand | Magnesium Metal-binding Pyridoxal phosphate |
| Molecular function | Decarboxylase Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | arginine catabolic process Inferred from electronic annotation. Source: InterPro putrescine biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW spermidine biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | arginine decarboxylase activity Inferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 658 | 658 | Biosynthetic arginine decarboxylase HAMAP MF_01417 | PRO_0000149962 | |||||
Regions | |||||||||
| Region | 307 – 317 | 11 | Substrate-binding Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 127 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG58069.1. BA000007 Genomic DNA. Translation: BAB37237.1. | |
| PIR | A85951. F91105. |
| RefSeq | NP_289510.1. NP_311841.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 916366. 958416. |
| GenomeReviews | Gene locus Z4283 in contig AE005174_GR. Gene locus ECs3814 in contig BA000007_GR. |
| KEGG | ece:Z4283. ecs:ECs3814. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8XCX9. |
| OMA | LICNGYK. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS3814-MON. |
Family and domain databases | |
| HAMAP | MF_01417. [Tree] |
| InterPro | IPR002985. Arg_decrbxlase. IPR000183. De-COase2. [Graphical view] |
| PANTHER | PTHR11482:SF3. Arg_decrbxlase. 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. |
| PROSITE | PS00878. ODR_DC_2_1. 1 hit. PS00879. ODR_DC_2_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SPEA_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8XCX9 | ||||||||
| Entry history |
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| 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


