NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-111.
STRAIN=AM1 / NCIMB 9133;
PubMed=8132470 [NCBI, ExPASy, EBI, Israel, Japan]
Morris C.J., Biville F., Turlin E., Lee E., Ellermann K., Fan W.H., Ramamoorthi R., Springer A.L., Lidstrom M.E.;
"Isolation, phenotypic characterization, and complementation analysis of mutants of Methylobacterium extorquens AM1 unable to synthesize pyrroloquinoline quinone and sequences of pqqD, pqqG, and pqqC.";
J. Bacteriol. 176:1746-1755(1994).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-372.
STRAIN=AM1 / NCIMB 9133;
PubMed=9043136 [NCBI, ExPASy, EBI, Israel, Japan]
Toyama H., Chistoserdova L., Lidstrom M.E.;
"Sequence analysis of pqq genes required for biosynthesis of pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the purification of a biosynthetic intermediate.";
Microbiology 143:595-602(1997).

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 (By similarity).
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 .
SIMILARITY: In the N-terminal section; belongs to the pqqC family.
SIMILARITY: In the C-terminal section; belongs to the pqqD 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

L25889; AAA17880.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U72662; AAB58899.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C55527; C55527.

3D structure databases

ModBase

Q49150.

Ontologies

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

Family and domain databases

HAMAP

MF_00654; fused; 1.
MF_00655; fused; 1.
PBIL [Tree]

InterPro

IPR016084; Haem_Oase-like_multi-hlx.
IPR011845; PQQ_synth_PqqC.
IPR008792; PQQ_synth_PqqD.
IPR004305; TENA/THI4/PQQ_synth_PqqC.
Graphical view of domain structure.

Gene3D

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

Pfam

PF05402; PqqD; 1.
PF03070; TENA_THI-4; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02111; PQQ_syn_pqqC; 1.

Other

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

Keywords

Oxidoreductase; PQQ biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 372`	`372`	`Bifunctional coenzyme PQQ synthesis protein C/D.`	`PRO_0000219980`
`REGION`	`1 267`	`267`	`PqqC.`
`REGION`	`268 280`	`13`	`Linker.`
`REGION`	`281 372`	`92`	`PqqD.`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 41577 Da [This is the MW of the unprocessed precursor]

CRC64: 3E502CEB4097695D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAQFPPPVP DTEQRLLSHE ELEAALRDIG ARRYHNLHPF HRLLHDGKLS KDQVRAWALN 

        70         80         90        100        110        120 
RYYYQAMIPV KDAALLARLP DAQLRRIWRQ RIVDHDGDHE GDGGIERWLK LAEGVGFTRD 

       130        140        150        160        170        180 
YVLSTKGILS ATRFSVDAYV HFVSERSLLE AIASSLTEMF SPTIISERVA GMLKNYDFIT 

       190        200        210        220        230        240 
KDTLAYFDKR LTQAPRDADF ALDYVKRHAT TPEMQRAAID ALTFKCNVLW TQLDALYFAY 

       250        260        270        280        290        300 
VAPGMVPPDA WQPGEGLVAE TNSAEDSPAA AASPAATTAE PTAFSGSDVP RLPRGVRLRF 

       310        320        330        340        350        360 
DEVRNKHVLL APERTFDLDD NAVAVLKLVD GRNTVSQIAQ ILGQTYDADP AIIEADILPM 

       370 
LAGLAQKRVL ER

Q49150 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