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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei351 – 3511Amidino-cysteine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

FAD, Flavoprotein, FMN

Enzyme and pathway databases

BioCyciPGIN242619:GHX8-1283-MONOMER.

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Propeptidei24 – 43201 PublicationPRO_0000001044Add
BLAST
Chaini44 – 556513Peptidylarginine deiminasePRO_0000001045Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi242619.PG1424.

Structurei

Secondary structure

1
556
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 576Combined sources
Beta strandi64 – 729Combined sources
Helixi77 – 8610Combined sources
Beta strandi89 – 957Combined sources
Helixi96 – 10914Combined sources
Helixi113 – 1153Combined sources
Beta strandi116 – 1205Combined sources
Helixi128 – 1314Combined sources
Beta strandi134 – 1385Combined sources
Turni139 – 1413Combined sources
Beta strandi142 – 15312Combined sources
Helixi155 – 1595Combined sources
Helixi161 – 1688Combined sources
Beta strandi172 – 1798Combined sources
Helixi181 – 1833Combined sources
Beta strandi188 – 1958Combined sources
Helixi197 – 2004Combined sources
Turni201 – 2044Combined sources
Helixi207 – 21812Combined sources
Beta strandi221 – 2266Combined sources
Beta strandi232 – 2343Combined sources
Helixi237 – 2393Combined sources
Beta strandi241 – 2455Combined sources
Beta strandi248 – 2536Combined sources
Helixi261 – 27212Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi283 – 2886Combined sources
Beta strandi299 – 3013Combined sources
Beta strandi304 – 3096Combined sources
Helixi313 – 32614Combined sources
Beta strandi331 – 3366Combined sources
Beta strandi339 – 3413Combined sources
Helixi350 – 3523Combined sources
Beta strandi354 – 3574Combined sources
Beta strandi362 – 3665Combined sources
Beta strandi371 – 3733Combined sources
Beta strandi379 – 3868Combined sources
Beta strandi392 – 40110Combined sources
Beta strandi408 – 4114Combined sources
Beta strandi413 – 4164Combined sources
Beta strandi419 – 4235Combined sources
Beta strandi432 – 44110Combined sources
Beta strandi446 – 4505Combined sources
Beta strandi458 – 4625Combined sources

3D structure databases

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

Enzyme and pathway databases

BioCyciPGIN242619:GHX8-1283-MONOMER.

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: September 7, 2016
This is version 76 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.