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P27505 (PQQC_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyrroloquinoline-quinone synthase
EC=1.3.3.11
Alternative name(s):
Coenzyme PQQ synthesis protein C
Pyrroloquinoline quinone biosynthesis protein C
Gene names
Name:pqqC
OrganismKlebsiella pneumoniae
Taxonomic identifier573 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

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. HAMAP-Rule MF_00654

Pathway

Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis. HAMAP-Rule MF_00654

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the PqqC family.

Ontologies

Keywords
   Biological processPQQ biosynthesis
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processpyrroloquinoline quinone biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionpyrroloquinoline-quinone synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Pyrroloquinoline-quinone synthase HAMAP-Rule MF_00654
PRO_0000219979

Secondary structure

1 ................................. 251
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27505 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: B48A494FA63B6598

FASTA25128,986
        10         20         30         40         50         60 
MLITDTLSPQ AFEEALRAKG AFYHIHHPYH IAMHNGDATR KQIQGWVANR FYYQTTIPLK 

        70         80         90        100        110        120 
DAAIMANCPD AQTRRKWVQR ILDHDGSHGE DGGIEAWLRL GEAVGLSRDD LLSERHVLPG 

       130        140        150        160        170        180 
VRFAVDAYLN FARRACWQEA ACSSLTELFA PQIHQSRLDS WPQHYPWIKE EGYFYFRSRL 

       190        200        210        220        230        240 
SQANRDVEHG LALAKAYCDS AEKQNRMLEI LQFKLDILWS MLDAMTMAYA LQRPPYHTVT 

       250 
DKAAWHTTRL V

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X58778 Genomic DNA. Translation: CAA41581.1.
PIRS20455.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OTVX-ray2.10A/B1-251[»]
1OTWX-ray2.30A/B1-251[»]
ProteinModelPortalP27505.
SMRP27505. Positions 1-251.
ModBaseSearch...

2D gel databases

UCD-2DPAGEP27505.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15352.
BRENDA1.3.3.11. 2814.
UniPathwayUPA00539.

Family and domain databases

Gene3D1.20.910.10. 1 hit.
HAMAPMF_00654. PQQ_syn_PqqC.
InterProIPR016084. Haem_Oase-like_multi-hlx.
IPR011845. PQQ_synth_PqqC.
IPR004305. Thiaminase-2/PQQC.
[Graphical view]
PfamPF03070. TENA_THI-4. 1 hit.
[Graphical view]
SUPFAMSSF48613. Heme_oxygenase. 1 hit.
TIGRFAMsTIGR02111. PQQ_syn_pqqC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP27505.

Entry information

Entry namePQQC_KLEPN
AccessionPrimary (citable) accession number: P27505
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 29, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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