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P27505

- PQQC_KLEPN

UniProt

P27505 - PQQC_KLEPN

Protein

Pyrroloquinoline-quinone synthase

Gene

pqqC

Organism
Klebsiella pneumoniae
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Ring cyclization and eight-electron oxidation of 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic-acid to PQQ.1 Publication

    Catalytic activityi

    6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 = 4,5-dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H2O2 + 2 H2O.

    Pathwayi

    GO - Molecular functioni

    1. pyrroloquinoline-quinone synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. pyrroloquinoline quinone biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    PQQ biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15352.
    BRENDAi1.3.3.11. 2814.
    UniPathwayiUPA00539.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyrroloquinoline-quinone synthase (EC:1.3.3.11)
    Alternative name(s):
    Coenzyme PQQ synthesis protein C
    Pyrroloquinoline quinone biosynthesis protein C
    Gene namesi
    Name:pqqC
    OrganismiKlebsiella pneumoniae
    Taxonomic identifieri573 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 251251Pyrroloquinoline-quinone synthasePRO_0000219979Add
    BLAST

    2D gel databases

    UCD-2DPAGEP27505.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    251
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 1810
    Helixi19 – 224
    Helixi24 – 263
    Helixi28 – 347
    Helixi40 – 6627
    Helixi71 – 8515
    Beta strandi87 – 904
    Helixi93 – 10311
    Helixi108 – 1125
    Helixi119 – 13416
    Helixi137 – 1426
    Helixi143 – 1497
    Turni162 – 1643
    Helixi170 – 18112
    Helixi189 – 1979
    Helixi201 – 22929
    Turni235 – 2395

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OTVX-ray2.10A/B1-251[»]
    1OTWX-ray2.30A/B1-251[»]
    ProteinModelPortaliP27505.
    SMRiP27505. Positions 1-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27505.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PqqC family.Curated

    Family and domain databases

    Gene3Di1.20.910.10. 1 hit.
    HAMAPiMF_00654. PQQ_syn_PqqC.
    InterProiIPR016084. Haem_Oase-like_multi-hlx.
    IPR011845. PQQ_synth_PqqC.
    IPR004305. Thiaminase-2/PQQC.
    [Graphical view]
    PfamiPF03070. TENA_THI-4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48613. SSF48613. 1 hit.
    TIGRFAMsiTIGR02111. PQQ_syn_pqqC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P27505-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLITDTLSPQ AFEEALRAKG AFYHIHHPYH IAMHNGDATR KQIQGWVANR    50
    FYYQTTIPLK DAAIMANCPD AQTRRKWVQR ILDHDGSHGE DGGIEAWLRL 100
    GEAVGLSRDD LLSERHVLPG VRFAVDAYLN FARRACWQEA ACSSLTELFA 150
    PQIHQSRLDS WPQHYPWIKE EGYFYFRSRL SQANRDVEHG LALAKAYCDS 200
    AEKQNRMLEI LQFKLDILWS MLDAMTMAYA LQRPPYHTVT DKAAWHTTRL 250
    V 251
    Length:251
    Mass (Da):28,986
    Last modified:August 1, 1992 - v1
    Checksum:iB48A494FA63B6598
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58778 Genomic DNA. Translation: CAA41581.1.
    PIRiS20455.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58778 Genomic DNA. Translation: CAA41581.1 .
    PIRi S20455.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OTV X-ray 2.10 A/B 1-251 [» ]
    1OTW X-ray 2.30 A/B 1-251 [» ]
    ProteinModelPortali P27505.
    SMRi P27505. Positions 1-251.
    ModBasei Search...
    MobiDBi Search...

    2D gel databases

    UCD-2DPAGE P27505.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00539 .
    BioCyci MetaCyc:MONOMER-15352.
    BRENDAi 1.3.3.11. 2814.

    Miscellaneous databases

    EvolutionaryTracei P27505.

    Family and domain databases

    Gene3Di 1.20.910.10. 1 hit.
    HAMAPi MF_00654. PQQ_syn_PqqC.
    InterProi IPR016084. Haem_Oase-like_multi-hlx.
    IPR011845. PQQ_synth_PqqC.
    IPR004305. Thiaminase-2/PQQC.
    [Graphical view ]
    Pfami PF03070. TENA_THI-4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48613. SSF48613. 1 hit.
    TIGRFAMsi TIGR02111. PQQ_syn_pqqC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and structure of the Klebsiella pneumoniae pqq operon."
      Meulenberg J.J.M., Sellink E., Riegman N.H., Postma P.W.
      Mol. Gen. Genet. 232:284-294(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418.
    2. "Synthesis of pyrroloquinoline quinone in vivo and in vitro and detection of an intermediate in the biosynthetic pathway."
      Velterop J.S., Sellink E., Meulenberg J.J., David S., Bulder I., Postma P.W.
      J. Bacteriol. 177:5088-5098(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418.
    3. "Quinone biogenesis: structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone."
      Magnusson O.T., Toyama H., Saeki M., Rojas A., Reed J.C., Liddington R.C., Klinman J.P., Schwarzenbacher R.
      Proc. Natl. Acad. Sci. U.S.A. 101:7913-7918(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiPQQC_KLEPN
    AccessioniPrimary (citable) accession number: P27505
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 71 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3