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

AE004091; AAG05375.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C83397; C83397.

RefSeq

NP_250677.1; -.

3D structure databases

SMR

Q9I2C2; 11-245.

ModBase

Q9I2C2.

Enzyme and pathway databases

BioCyc

PAER208964:PA1987-MON; -.

Organism-specific databases

PseudoCAP

PA1987; -.

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

Q9I2C2.

Genome annotation databases

GeneID

879112; -.

GenomeReviews

AE004091_GR; PA1987.

KEGG

pae:PA1987; -.

Phylogenomic databases

HOGENOM

Q9I2C2; -.

Genome annotation databases

CMR

Q9I2C2; PA1987.

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`	`1 250`	`250`		`Pyrroloquinoline-quinone synthase.`	`PRO_0000219982`

Sequence information

Length: 250 AA [This is the length of the unprocessed precursor]

Molecular weight: 29449 Da [This is the MW of the unprocessed precursor]

CRC64: 6245E87D0C200E46 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRAAMDRAE FERALRDKGR YYHIHHPFHV AMYEGRASRE QIQGWVANRF YYQVNIPLKD 

        70         80         90        100        110        120 
AAILANCPDR EVRREWIQRI LDHDGAPGEA GGIEAWLRLA EAVGLEREQV LSEERVLPGV 

       130        140        150        160        170        180 
RFAVDAYVNF ARRASWQEAA SSSLTELFAP QIHQSRLDSW PRHYPWIEAA GYEYFRSRLA 

       190        200        210        220        230        240 
QARRDVEHGL RITLEHYRTR EAQERMLDIL QFKLDVLWSM LDAMSMAYEL ERPPYHTVTR 

       250 
ERVWHRGLAS

Q9I2C2 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