ID   PQQC_RHOS5              Reviewed;         255 AA.
AC   A4WPI0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
DE   RecName: Full=Pyrroloquinoline-quinone synthase;
DE            EC=1.3.3.11;
DE   AltName: Full=Coenzyme PQQ synthesis protein C;
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein C;
GN   Name=pqqC; OrderedLocusNames=Rsph17025_0388;
OS   Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=349102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC
RT   17025.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ring cyclization and eight-electron oxidation of 3a-(2-
CC       amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-
CC       7,9-dicarboxylic-acid to PQQ (By similarity).
CC   -!- CATALYTIC ACTIVITY: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-
CC       1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O(2) = 4,5-
CC       dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate
CC       + 2 H(2)O(2) + 2 H(2)O.
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the pqqC family.
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DR   EMBL; CP000661; ABP69294.1; -; Genomic_DNA.
DR   RefSeq; YP_001166599.1; -.
DR   GeneID; 5082224; -.
DR   GenomeReviews; CP000661_GR; Rsph17025_0388.
DR   KEGG; rsq:Rsph17025_0388; -.
DR   OMA; A4WPI0; AWALNRY.
DR   GO; GO:0033732; F:pyrroloquinoline-quinone synthase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00654; -; 1.
DR   InterPro; IPR011845; PQQ_synth_PqqC.
DR   InterPro; IPR004305; TENA/THI4/PQQ_synth_PqqC.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   TIGRFAMs; TIGR02111; PQQ_syn_pqqC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Oxidoreductase; PQQ biosynthesis.
FT   CHAIN         1    255       Pyrroloquinoline-quinone synthase.
FT                                /FTId=PRO_1000061679.
SQ   SEQUENCE   255 AA;  29089 MW;  E789A491EC3D8435 CRC64;
     MSLDLTPTLS PARPLDSADA MEDRLREIGA ARYHDRHPFH HLLHGGQLTR GQVQAWALNR
     YYYQCSIPVK DAVVISRFRD RATRVEWRHR LEDHDGAEGT EGGIDRWLVL TDALGLDRDY
     VEATDGILPA TRFAVDAYVH FVRDQSPLEA IASCLTELFA PHIHAERISG MLAHYDFVNP
     TVMAYFQRRL SQAPRDADYA LRYVREHART PQERAAVCNA LIFKTQVLWT QLDALHHAYV
     LGHVPPGAFV PEDMR
//