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Q9RQJ2 (PAD_PORGI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidylarginine deiminase

EC=3.5.3.-
Gene names
Ordered Locus Names:PG_1424
OrganismPorphyromonas gingivalis (strain ATCC BAA-308 / W83) [Complete proteome] [HAMAP]
Taxonomic identifier242619 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length556 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentSecreted
   DomainSignal
   LigandFAD
Flavoprotein
FMN
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processputrescine biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein-arginine deiminase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 4320 Probable
PRO_0000001044
Chain44 – 556513Peptidylarginine deiminase
PRO_0000001045

Sites

Active site3511Amidino-cysteine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RQJ2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6E189E508868DCF6

FASTA55661,730
        10         20         30         40         50         60 
MKKLLQAKAL ILALGLFQLP AIAQTQMQAD RTNGQFATEE MQRAFQETNP PAGPVRAIAE 

        70         80         90        100        110        120 
YERSAAVLVR YPFGIPMELI KELAKNDKVI TIVASESQKN TVITQYTQSG VNLSNCDFII 

       130        140        150        160        170        180 
AKTDSYWTRD YTGWFAMYDT NKVGLVDFIY NRPRPNDDEF PKYEAQYLGI EMFGMKLKQT 

       190        200        210        220        230        240 
GGNYMTDGYG SAVQSHIAYT ENSSLSQAQV NQKMKDYLGI THHDVVQDPN GEYINHVDCW 

       250        260        270        280        290        300 
GKYLAPNKIL IRKVPDNHPQ HQALEDMAAY FAAQTCAWGT KYEVYRALAT NEQPYTNSLI 

       310        320        330        340        350        360 
LNNRVFVPVN GPASVDNDAL NVYKTAMPGY EIIGVKGASG TPWLGTDALH CRTHEVADKG 

       370        380        390        400        410        420 
YLYIKHYPIL GEQAGPDYKI EADVVSCANA TISPVQCYYR INGSGSFKAA DMTMESTGHY 

       430        440        450        460        470        480 
TYSFTGLNKN DKVEYYISAA DNSGRKETYP FIGEPDPFKF TCMNETNTCT VTGAAKALRA 

       490        500        510        520        530        540 
WFNAGRSELA VSVSLNIAGT YRIKLYNTAG EEVAAMTKEL VAGTSVFSMD VYSQAPGTYV 

       550 
LVVEGNGIRE TMKILK 

« Hide

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. expand/collapse author list , Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., 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.
RefSeqNP_905579.1. NC_002950.2.

3D structure databases

ProteinModelPortalQ9RQJ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING242619.PG1424.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ66478; AAQ66478; PG_1424.
GeneID2552184.
KEGGpgi:PG1424.
PATRIC22979880. VBIPorGin134034_1324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2957.
OMARTRAVWD.
OrthoDBEOG6716HM.

Enzyme and pathway databases

BioCycPGIN242619:GHX8-1283-MONOMER.

Family and domain databases

InterProIPR007466. Peptidyl-Arg-deiminase_porph.
[Graphical view]
PfamPF04371. PAD_porph. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePAD_PORGI
AccessionPrimary (citable) accession number: Q9RQJ2
Secondary accession number(s): Q7BW72
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families