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Q9RQJ2

- PAD_PORGI

UniProt

Q9RQJ2 - PAD_PORGI

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
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    FAD or FMN.Curated

    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

    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-SubCell

    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

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    MKKLLQAKAL ILALGLFQLP AIAQTQMQAD RTNGQFATEE MQRAFQETNP    50
    PAGPVRAIAE YERSAAVLVR YPFGIPMELI KELAKNDKVI TIVASESQKN 100
    TVITQYTQSG VNLSNCDFII AKTDSYWTRD YTGWFAMYDT NKVGLVDFIY 150
    NRPRPNDDEF PKYEAQYLGI EMFGMKLKQT GGNYMTDGYG SAVQSHIAYT 200
    ENSSLSQAQV NQKMKDYLGI THHDVVQDPN GEYINHVDCW GKYLAPNKIL 250
    IRKVPDNHPQ HQALEDMAAY FAAQTCAWGT KYEVYRALAT NEQPYTNSLI 300
    LNNRVFVPVN GPASVDNDAL NVYKTAMPGY EIIGVKGASG TPWLGTDALH 350
    CRTHEVADKG YLYIKHYPIL GEQAGPDYKI EADVVSCANA TISPVQCYYR 400
    INGSGSFKAA DMTMESTGHY TYSFTGLNKN DKVEYYISAA DNSGRKETYP 450
    FIGEPDPFKF TCMNETNTCT VTGAAKALRA WFNAGRSELA VSVSLNIAGT 500
    YRIKLYNTAG EEVAAMTKEL VAGTSVFSMD VYSQAPGTYV LVVEGNGIRE 550
    TMKILK 556
    Length:556
    Mass (Da):61,730
    Last modified:May 1, 2000 - v1
    Checksum:i6E189E508868DCF6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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

    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: October 1, 2014
    This is version 67 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