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Q9RQJ2

- PAD_PORGI

UniProt

Q9RQJ2 - PAD_PORGI

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Protein

Peptidylarginine deiminase

Gene

PG_1424

Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Status
Reviewed - 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

Vmax=104 nmol/min/mg enzyme with Benzoyl-L-arginine as substrate1 Publication

Vmax=186 nmol/min/mg enzyme with Benzoylglycyl-L-arginine as substrate1 Publication

Vmax=77 nmol/min/mg enzyme with BAA as substrate1 Publication

Vmax=90 nmol/min/mg enzyme with BAEE as substrate1 Publication

Vmax=26 nmol/min/mg enzyme with L-arginine as substrate1 Publication

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

  1. protein-arginine deiminase activity Source: InterPro

GO - Biological processi

  1. putrescine biosynthetic process Source: InterPro
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
ProteomesiUP000000588: Chromosome

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
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

3D structure databases

ProteinModelPortaliQ9RQJ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the agmatine deiminase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2957.
OMAiRTRAVWD.
OrthoDBiEOG6716HM.

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.
RefSeqiNP_905579.1. NC_002950.2.
WP_005873463.1. NC_002950.2.

Genome annotation databases

EnsemblBacteriaiAAQ66478; AAQ66478; PG_1424.
GeneIDi2552184.
KEGGipgi:PG1424.
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 .
RefSeqi NP_905579.1. NC_002950.2.
WP_005873463.1. NC_002950.2.

3D structure databases

ProteinModelPortali Q9RQJ2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 242619.PG1424.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAQ66478 ; AAQ66478 ; PG_1424 .
GeneIDi 2552184.
KEGGi pgi:PG1424.
PATRICi 22979880. VBIPorGin134034_1324.

Phylogenomic databases

eggNOGi COG2957.
OMAi RTRAVWD.
OrthoDBi EOG6716HM.

Enzyme and pathway databases

BioCyci PGIN242619:GHX8-1283-MONOMER.

Family and domain databases

InterProi IPR007466. Peptidyl-Arg-deiminase_porph.
[Graphical view ]
Pfami PF04371. PAD_porph. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-308 / W83.

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 26, 2014
This is version 69 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3