Q9K0U3 (SPEA_NEIMB) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 69.
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: Biosynthetic arginine decarboxylase Short name=ADC EC=4.1.1.19 | ||||
| Gene names |
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| Organism | Neisseria meningitidis serogroup B | ||||
| Taxonomic identifier | 491 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 630 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 |
| Catalytic activity | L-arginine = agmatine + CO2. HAMAP MF_01417 |
| Cofactor | Magnesium By similarity. HAMAP MF_01417 Pyridoxal phosphate By similarity. HAMAP MF_01417 |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Polyamine biosynthesis Putrescine biosynthesis Spermidine biosynthesis |
| Ligand | Magnesium Metal-binding Pyridoxal phosphate |
| Molecular function | Decarboxylase Lyase |
| Technical term | Complete proteome Reference 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: UniProtKB-KW |
| Molecular function | arginine decarboxylase activity Inferred from electronic annotation. Source: EC 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 | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 630 | 630 | Biosynthetic arginine decarboxylase HAMAP MF_01417 | PRO_0000149965 | |||||
Regions | |||||||||
| Region | 279 – 289 | 11 | Substrate-binding Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 99 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. Venter J.C.Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE002098 Genomic DNA. Translation: AAF40905.1. |
| PIR | A81196. |
| RefSeq | NP_273515.1. NC_003112.2. |
3D structure databases | |
| ProteinModelPortal | Q9K0U3. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBNEIT00000009390; EBNEIP00000009010; EBNEIG00000009390. |
| GeneID | 902584. |
| GenomeReviews | Gene locus NMB0468 in contig AE002098_GR. |
| KEGG | nme:NMB0468. |
| NMPDR | fig|122586.1.peg.449. |
| PATRIC | 20356184. VBINeiMen85645_0613. |
| TIGR | NMB0468. |
Phylogenomic databases | |
| GeneTree | EBGT00050000021104. |
| HOGENOM | HBG321436. |
| OMA | LICNGYK. |
| ProtClustDB | PRK05354. |
Enzyme and pathway databases | |
| BioCyc | NMEN122586:NMB_0468-MONOMER. |
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] |
| Gene3D | G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 2 hits. |
| 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 | SPEA_NEIMB | ||||||||
| Accession | Primary (citable) accession number: Q9K0U3 | ||||||||
| 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 |

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