Q9RQJ2 (PAD_PORGI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 60.
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: Peptidylarginine deiminase EC=3.5.3.- | ||
| Gene names |
| ||
| Organism | Porphyromonas gingivalis (strain ATCC BAA-308 / W83) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 242619 [NCBI] | ||
| Taxonomic lineage | Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Porphyromonadaceae › Porphyromonas › ![]() |
Protein attributes
| Sequence length | 556 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Deiminates the guanidino group of C-terminal arginine residues on a variety of peptides, including the vasoregulatory peptide-hormone bradykinin, to yield ammonia and a citrulline residue. May promote the growth of the pathogen in the periodontal pocket by producing ammonia, ammonia having a protective effect during acidic cleaning cycles in the mouth. Ref.1 |
| Cofactor | FAD or FMN Potential. Ref.1 |
| Enzyme regulation | Inhibited by cysteine and TLCK. Inhibited by high concentration of thiourea and thio-L-citrulline. Ref.1 |
| Subcellular location | Secreted Potential. |
| Sequence similarities | Belongs to the agmatine deiminase family. |
| Biophysicochemical properties | Kinetic parameters: KM=2.9 µM for Benzoyl-L-arginine Ref.1 KM=28 µM for Benzoylglycyl-L-arginine KM=152 µM for BAA KM=874 µM for BAEE KM=141 µM for L-arginine KM=47 µM for BK Vmax=104 nmol/min/mg enzyme with Benzoyl-L-arginine as substrate Vmax=186 nmol/min/mg enzyme with Benzoylglycyl-L-arginine as substrate Vmax=77 nmol/min/mg enzyme with BAA as substrate Vmax=90 nmol/min/mg enzyme with BAEE as substrate Vmax=26 nmol/min/mg enzyme with L-arginine as substrate Vmax=117 nmol/min/mg enzyme with BK as substrate pH dependence: Optimum pH is 9.3. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | FAD FMN |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | putrescine biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | protein-arginine deiminase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Purification, characterization, and sequence analysis of a potential virulence factor from Porphyromonas gingivalis, peptidylarginine deiminase." McGraw W.T., Potempa J., Farley D., Travis J. Infect. Immun. 67:3248-3256(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 44-73, FUNCTION, ENZYME ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, POSSIBLE COFACTOR. Strain: ATCC BAA-308 / W83. |
| [2] | "Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83." Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., Granger D., Tettelin H. Fraser C.M.J. Bacteriol. 185:5591-5601(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-308 / W83. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF100668 Genomic DNA. Translation: AAF06719.1. AE015924 Genomic DNA. Translation: AAQ66478.1. |
| RefSeq | NP_905579.1. NC_002950.2. |
3D structure databases | |
| ProteinModelPortal | Q9RQJ2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 242619.PG1424. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAQ66478; AAQ66478; PG_1424. |
| GeneID | 2552184. |
| KEGG | pgi:PG1424. |
| PATRIC | 22979880. VBIPorGin134034_1324. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2957. |
| OMA | HILQTEN. |
| ProtClustDB | CLSK647850. |
Enzyme and pathway databases | |
| BioCyc | PGIN242619:GHX8-1246-MONOMER. |
Family and domain databases | |
| InterPro | IPR007466. Peptidyl-Arg-deiminase_porph. [Graphical view] |
| Pfam | PF04371. PAD_porph. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PAD_PORGI | ||||||||
| Accession | Primary (citable) accession number: Q9RQJ2 Secondary accession number(s): Q7BW72 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
