[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIB 418; PubMed=1313537 [NCBI, ExPASy, EBI, Israel, Japan] Meulenberg J.J.M., Sellink E., Riegman N.H., Postma P.W.; "Nucleotide sequence and structure of the Klebsiella pneumoniae pqq operon."; Mol. Gen. Genet. 232:284-294(1992).
[2]	FUNCTION. STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIB 418; PubMed=7665488 [NCBI, ExPASy, EBI, Israel, Japan] Velterop J.S., Sellink E., Meulenberg J.J., David S., Bulder I., Postma P.W.; "Synthesis of pyrroloquinoline quinone in vivo and in vitro and detection of an intermediate in the biosynthetic pathway."; J. Bacteriol. 177:5088-5098(1995).
[3]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT. DOI=10.1073/pnas.0402640101; PubMed=15148379 [NCBI, ExPASy, EBI, Israel, Japan] Magnusson O.T., Toyama H., Saeki M., Rojas A., Reed J.C., Liddington R.C., Klinman J.P., Schwarzenbacher R.; "Quinone biogenesis: structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone."; Proc. Natl. Acad. Sci. U.S.A. 101:7913-7918(2004).

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.
CATALYTIC ACTIVITY: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate + 3 O₂ = 4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H₂O₂ + 2 H₂O.
PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis .
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the pqqC family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X58778; CAA41581.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S20455; S20455.

3D structure databases

PDB

1OTV; X-ray; 2.10 A; A/B=1-251.	[ExPASy / RCSB / EBI]
1OTW; X-ray; 2.30 A; A/B=1-251.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1OTV; -.
1OTW; -.

ModBase

P27505.

Ontologies

GO:0018189;	Biological process: pyrroloquinoline quinone biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00654; -; 1.
PBIL [Tree]

InterPro

IPR016084; Haem_Oase-like_multi-hlx.
IPR011845; PQQ_synth_PqqC.
IPR004305; TENA/THI4/PQQ_synth_PqqC.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.910.10; Haem_Oase-like_multi-hlx; 1.

Pfam

PF03070; TENA_THI-4; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02111; PQQ_syn_pqqC; 1.

Other

P27505; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Oxidoreductase; PQQ biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 251`	`251`	`Pyrroloquinoline-quinone synthase.`	`PRO_0000219979`
`HELIX`	`9 18`	`10`
`HELIX`	`19 22`	`4`
`HELIX`	`24 26`	`3`
`HELIX`	`28 34`	`7`
`HELIX`	`40 66`	`27`
`HELIX`	`71 85`	`15`
`HELIX`	`93 103`	`11`
`HELIX`	`108 112`	`5`
`HELIX`	`119 134`	`16`
`HELIX`	`137 142`	`6`
`HELIX`	`143 149`	`7`
`TURN`	`162 164`	`3`
`HELIX`	`170 181`	`12`
`HELIX`	`189 197`	`9`
`HELIX`	`201 229`	`29`
`TURN`	`235 239`	`5`

Sequence information

Length: 251 AA [This is the length of the unprocessed precursor]

Molecular weight: 28986 Da [This is the MW of the unprocessed precursor]

CRC64: B48A494FA63B6598 [This is a checksum on the sequence]

        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

P27505 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools