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Protein

Pyrroloquinoline-quinone synthase

Gene

pqqC

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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-HAMAP
Complete GO annotation...

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 – 1810Combined sources
Helixi19 – 224Combined sources
Helixi24 – 263Combined sources
Helixi28 – 347Combined sources
Helixi40 – 6627Combined sources
Helixi71 – 8515Combined sources
Beta strandi87 – 904Combined sources
Helixi93 – 10311Combined sources
Helixi108 – 1125Combined sources
Helixi119 – 13416Combined sources
Helixi137 – 1426Combined sources
Helixi143 – 1497Combined sources
Turni162 – 1643Combined sources
Helixi170 – 18112Combined sources
Helixi189 – 1979Combined sources
Helixi201 – 22929Combined sources
Turni235 – 2395Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MLITDTLSPQ AFEEALRAKG AFYHIHHPYH IAMHNGDATR KQIQGWVANR
60 70 80 90 100
FYYQTTIPLK DAAIMANCPD AQTRRKWVQR ILDHDGSHGE DGGIEAWLRL
110 120 130 140 150
GEAVGLSRDD LLSERHVLPG VRFAVDAYLN FARRACWQEA ACSSLTELFA
160 170 180 190 200
PQIHQSRLDS WPQHYPWIKE EGYFYFRSRL SQANRDVEHG LALAKAYCDS
210 220 230 240 250
AEKQNRMLEI LQFKLDILWS MLDAMTMAYA LQRPPYHTVT DKAAWHTTRL

V
Length:251
Mass (Da):28,986
Last modified:July 31, 1992 - v1
Checksum:iB48A494FA63B6598
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58778 Genomic DNA. Translation: CAA41581.1.
PIRiS20455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58778 Genomic DNA. Translation: CAA41581.1.
PIRiS20455.

3D structure databases

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

2D gel databases

UCD-2DPAGEP27505.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP27505.

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.
ProtoNetiSearch...

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(1991) [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(1994) [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(2003) [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: July 31, 1992
Last sequence update: July 31, 1992
Last modified: February 3, 2015
This is version 73 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

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 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.