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Protein

Peptidylarginine deiminase

Gene

PG_1424

Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

Enzyme 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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

FAD, Flavoprotein, FMN

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

Complete GO annotation...

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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi52 – 57Combined sources6
Beta strandi64 – 72Combined sources9
Helixi77 – 86Combined sources10
Beta strandi89 – 95Combined sources7
Helixi96 – 109Combined sources14
Helixi113 – 115Combined sources3
Beta strandi116 – 120Combined sources5
Helixi128 – 131Combined sources4
Beta strandi134 – 138Combined sources5
Turni139 – 141Combined sources3
Beta strandi142 – 153Combined sources12
Helixi155 – 159Combined sources5
Helixi161 – 168Combined sources8
Beta strandi172 – 179Combined sources8
Helixi181 – 183Combined sources3
Beta strandi188 – 195Combined sources8
Helixi197 – 200Combined sources4
Turni201 – 204Combined sources4
Helixi207 – 218Combined sources12
Beta strandi221 – 226Combined sources6
Beta strandi232 – 234Combined sources3
Helixi237 – 239Combined sources3
Beta strandi241 – 245Combined sources5
Beta strandi248 – 253Combined sources6
Helixi261 – 272Combined sources12
Beta strandi279 – 281Combined sources3
Beta strandi283 – 288Combined sources6
Beta strandi299 – 301Combined sources3
Beta strandi304 – 309Combined sources6
Helixi313 – 326Combined sources14
Beta strandi331 – 336Combined sources6
Beta strandi339 – 341Combined sources3
Helixi350 – 352Combined sources3
Beta strandi354 – 357Combined sources4
Beta strandi362 – 366Combined sources5
Beta strandi371 – 373Combined sources3
Beta strandi379 – 386Combined sources8
Beta strandi392 – 401Combined sources10
Beta strandi408 – 411Combined sources4
Beta strandi413 – 416Combined sources4
Beta strandi419 – 423Combined sources5
Beta strandi432 – 441Combined sources10
Beta strandi446 – 450Combined sources5
Beta strandi458 – 462Combined sources5

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...

Family & Domainsi

Sequence similaritiesi

Belongs to the agmatine deiminase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107VPC. Bacteria.
ENOG410ZPIS. LUCA.
OMAiRTRAVWD.

Family and domain databases

InterProiIPR007466. Peptidyl-Arg-deiminase_porph.
[Graphical view]
PfamiPF04371. PAD_porph. 1 hit.
[Graphical view]

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.
GeneIDi2552184.
KEGGipgi:PG_1424.
PATRICi22979880. VBIPorGin134034_1324.

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.
GeneIDi2552184.
KEGGipgi:PG_1424.
PATRICi22979880. VBIPorGin134034_1324.

Phylogenomic databases

eggNOGiENOG4107VPC. Bacteria.
ENOG410ZPIS. LUCA.
OMAiRTRAVWD.

Family and domain databases

InterProiIPR007466. Peptidyl-Arg-deiminase_porph.
[Graphical view]
PfamiPF04371. PAD_porph. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPAD_PORGI
AccessioniPrimary (citable) accession number: Q9RQJ2
Secondary accession number(s): Q7BW72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 77 of the entry and version 1 of the sequence. [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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.