Q3M7K6 (Q3M7K6_ANAVT) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 40.
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 MF_01417 Short name=ADC HAMAP MF_01417 EC=4.1.1.19 HAMAP MF_01417 | ||||
| Gene names |
| ||||
| Organism | Anabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 240292 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena |
Protein attributes
| Sequence length | 671 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP MF_01417 SAAS SAAS009006 |
| Catalytic activity | L-arginine = agmatine + CO2. HAMAP MF_01417 SAAS SAAS009006 RuleBase RU003740 |
| Cofactor | Magnesium By similarity. HAMAP MF_01417 RuleBase RU003740 SAAS SAAS009006 Pyridoxal phosphate By similarity. HAMAP MF_01417 SAAS SAAS000183 |
| Pathway | Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP MF_01417 |
| Sequence similarities | Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. HAMAP MF_01417 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Polyamine biosynthesis HAMAP MF_01417 SAAS SAAS009006 Spermidine biosynthesis HAMAP MF_01417 SAAS SAAS009006 RuleBase RU003740 |
| Ligand | Magnesium SAAS SAAS009006 HAMAP MF_01417 Metal-binding HAMAP MF_01417 SAAS SAAS009006 Pyridoxal phosphate HAMAP MF_01417 SAAS SAAS000183 |
| Molecular function | Decarboxylase HAMAP MF_01417 SAAS SAAS009006 RuleBase RU003740 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 | 323 – 333 | 11 | Substrate-binding By similarity HAMAP MF_01417 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 141 | 1 | N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01417 | ||||||
Sequences
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References
| [1] | "Complete sequence of Anabaena variabilis ATCC 29413." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29413 / PCC 7937. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000117 Genomic DNA. Translation: ABA23030.1. |
| RefSeq | YP_323925.1. NC_007413.1. |
3D structure databases | |
| ProteinModelPortal | Q3M7K6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q3M7K6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3679949. |
| GenomeReviews | Gene locus Ava_3423 in contig CP000117_GR. |
| KEGG | ava:Ava_3423. |
| NMPDR | fig|240292.3.peg.3973. |
| PATRIC | 35427937. VBIAnaVar43351_4501. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1166. |
| HOGENOM | HBG321436. |
| OMA | LICNGYK. |
| PhylomeDB | Q3M7K6. |
| ProtClustDB | PRK05354. |
Family and domain databases | |
| HAMAP | MF_01417. SpeA. [Tree] |
| InterPro | IPR009006. Ala_racemase/Decarboxylase_C. IPR002985. Arg_decrbxlase. IPR022643. De-COase2_C. IPR022657. De-COase2_CS. IPR022644. De-COase2_N. IPR022653. De-COase2_pyr-phos_BS. IPR000183. Orn/DAP/Arg_de-COase. [Graphical view] |
| KO | K01585. |
| 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. |
| SUPFAM | SSF50621. Racem_decarbox_C. 1 hit. |
| 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 | Q3M7K6_ANAVT | ||||||||
| Accession | Primary (citable) accession number: Q3M7K6 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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