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Protein

Peptidylarginine deiminase

Gene

PG_1424

Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

Cofactori

FADCurated, FMNCurated

Activity regulationi

Inhibited by cysteine and TLCK. Inhibited by high concentration of thiourea and thio-L-citrulline.1 Publication

Kineticsi

  1. KM=2.9 µM for Benzoyl-L-arginine1 Publication
  2. KM=28 µM for Benzoylglycyl-L-arginine1 Publication
  3. KM=152 µM for BAA1 Publication
  4. KM=874 µM for BAEE1 Publication
  5. KM=141 µM for L-arginine1 Publication
  6. KM=47 µM for BK1 Publication
  1. Vmax=104 nmol/min/mg enzyme with Benzoyl-L-arginine as substrate1 Publication
  2. Vmax=186 nmol/min/mg enzyme with Benzoylglycyl-L-arginine as substrate1 Publication
  3. Vmax=77 nmol/min/mg enzyme with BAA as substrate1 Publication
  4. Vmax=90 nmol/min/mg enzyme with BAEE as substrate1 Publication
  5. Vmax=26 nmol/min/mg enzyme with L-arginine as substrate1 Publication
  6. Vmax=117 nmol/min/mg enzyme with BK as substrate1 Publication

pH dependencei

Optimum pH is 9.3.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei351Amidino-cysteine intermediateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandFAD, Flavoprotein, FMN

Enzyme and pathway databases

SABIO-RKiQ9RQJ2

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidylarginine deiminase (EC:3.5.3.-)
Gene namesi
Ordered Locus Names:PG_1424
OrganismiPorphyromonas gingivalis (strain ATCC BAA-308 / W83)
Taxonomic identifieri242619 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas
Proteomesi
  • UP000000588 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
PropeptideiPRO_000000104424 – 431 PublicationAdd BLAST20
ChainiPRO_000000104544 – 556Peptidylarginine deiminaseAdd BLAST513

Interactioni

Protein-protein interaction databases

STRINGi242619.PG1424

Structurei

Secondary structure

1556
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9RQJ2
SMRiQ9RQJ2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the agmatine deiminase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107VPC Bacteria
ENOG410ZPIS LUCA
OMAiGNYMSDG

Family and domain databases

InterProiView protein in InterPro
IPR007466 Peptidyl-Arg-deiminase_porph
PANTHERiPTHR31377 PTHR31377, 1 hit
PfamiView protein in Pfam
PF04371 PAD_porph, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9RQJ2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKLLQAKAL ILALGLFQLP AIAQTQMQAD RTNGQFATEE MQRAFQETNP
60 70 80 90 100
PAGPVRAIAE YERSAAVLVR YPFGIPMELI KELAKNDKVI TIVASESQKN
110 120 130 140 150
TVITQYTQSG VNLSNCDFII AKTDSYWTRD YTGWFAMYDT NKVGLVDFIY
160 170 180 190 200
NRPRPNDDEF PKYEAQYLGI EMFGMKLKQT GGNYMTDGYG SAVQSHIAYT
210 220 230 240 250
ENSSLSQAQV NQKMKDYLGI THHDVVQDPN GEYINHVDCW GKYLAPNKIL
260 270 280 290 300
IRKVPDNHPQ HQALEDMAAY FAAQTCAWGT KYEVYRALAT NEQPYTNSLI
310 320 330 340 350
LNNRVFVPVN GPASVDNDAL NVYKTAMPGY EIIGVKGASG TPWLGTDALH
360 370 380 390 400
CRTHEVADKG YLYIKHYPIL GEQAGPDYKI EADVVSCANA TISPVQCYYR
410 420 430 440 450
INGSGSFKAA DMTMESTGHY TYSFTGLNKN DKVEYYISAA DNSGRKETYP
460 470 480 490 500
FIGEPDPFKF TCMNETNTCT VTGAAKALRA WFNAGRSELA VSVSLNIAGT
510 520 530 540 550
YRIKLYNTAG EEVAAMTKEL VAGTSVFSMD VYSQAPGTYV LVVEGNGIRE

TMKILK
Length:556
Mass (Da):61,730
Last modified:May 1, 2000 - v1
Checksum:i6E189E508868DCF6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF100668 Genomic DNA Translation: AAF06719.1
AE015924 Genomic DNA Translation: AAQ66478.1
RefSeqiWP_005873463.1, NC_002950.2

Genome annotation databases

EnsemblBacteriaiAAQ66478; AAQ66478; PG_1424
GeneIDi29256112
KEGGipgi:PG_1424

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF100668 Genomic DNA Translation: AAF06719.1
AE015924 Genomic DNA Translation: AAQ66478.1
RefSeqiWP_005873463.1, NC_002950.2

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4YT9X-ray1.50A44-475[»]
4YTBX-ray1.40A44-475[»]
4YTGX-ray1.80A44-475[»]
5AK7X-ray1.46A49-484[»]
5AK8X-ray1.48A49-484[»]
ProteinModelPortaliQ9RQJ2
SMRiQ9RQJ2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi242619.PG1424

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ66478; AAQ66478; PG_1424
GeneIDi29256112
KEGGipgi:PG_1424

Phylogenomic databases

eggNOGiENOG4107VPC Bacteria
ENOG410ZPIS LUCA
OMAiGNYMSDG

Enzyme and pathway databases

SABIO-RKiQ9RQJ2

Family and domain databases

InterProiView protein in InterPro
IPR007466 Peptidyl-Arg-deiminase_porph
PANTHERiPTHR31377 PTHR31377, 1 hit
PfamiView protein in Pfam
PF04371 PAD_porph, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPAD_PORGI
AccessioniPrimary (citable) accession number: Q9RQJ2
Secondary accession number(s): Q7BW72
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 1, 2000
Last modified: September 12, 2018
This is version 82 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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