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 (By similarity).
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.
PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis .
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

CP000075; AAY39699.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_237737.1; -.

3D structure databases

SMR

Q4ZMC3; 7-246.

ModBase

Q4ZMC3.

Enzyme and pathway databases

BioCyc

PSYR205918:PSYR_4672-MON; -.

Ontologies

GO:0033732;	Molecular function: pyrroloquinoline-quinone synthase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

Q4ZMC3.

Genome annotation databases

GeneID

3370222; -.

GenomeReviews

CP000075_GR; Psyr_4672.

KEGG

psb:Psyr_4672; -.

NMPDR

fig|205918.4.peg.3735; -.

Phylogenomic databases

HOGENOM

Q4ZMC3; -.

Genome annotation databases

CMR

Q4ZMC3; Psyr_4672.

Other

UniRef

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

Keywords

Complete proteome; Oxidoreductase; PQQ biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 251`	`251`		`Pyrroloquinoline-quinone synthase.`	`PRO_1000061676`

Sequence information

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

Molecular weight: 29117 Da [This is the MW of the unprocessed precursor]

CRC64: E5FCA799BA306006 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEATALSPA EFEQALRAKG AYYHIYHPFH VAMYEGRATR EQIQGWVANR FYYQVNIPLK 

        70         80         90        100        110        120 
DAAILANCPD REIRREWIQR LLDHDGAPGE DGGIEAWLRL GQAVGLDPDQ LRSQELVLPG 

       130        140        150        160        170        180 
VRFAVDAYVN FARRANWQEA ASSSLTELFA PQIHQSRLDS WPQHYPWIDP AGYEYFRTRL 

       190        200        210        220        230        240 
GQARRDVEHG LAITLQHYTT YEGQQRMLEI LQFKLDILWS MLDAMSMAYE LNRPPYHSVT 

       250 
DQRVWHKGIT L

Q4ZMC3 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