ID PQQC_PSEPG Reviewed; 251 AA. AC B0KJ68; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 1. DT 16-JUN-2009, entry version 10. 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=PputGB1_0407; OS Pseudomonas putida (strain GB-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=76869; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.; RT "Complete sequence of Pseudomonas putida GB-1."; RL Submitted (JAN-2008) 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000926; ABY96318.1; -; Genomic_DNA. DR RefSeq; YP_001666654.1; -. DR GeneID; 5868145; -. DR GenomeReviews; CP000926_GR; PputGB1_0407. DR KEGG; ppg:PputGB1_0407; -. DR OMA; B0KJ68; DSWPQHY. 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; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR011845; PQQ_synth_PqqC. DR InterPro; IPR004305; TENA/THI4/PQQ_synth_PqqC. DR Gene3D; G3DSA:1.20.910.10; Haem_Oase-like_multi-hlx; 1. 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 1 251 Pyrroloquinoline-quinone synthase. FT /FTId=PRO_1000082784. SQ SEQUENCE 251 AA; 29061 MW; A9D301FD33C74E58 CRC64; MSDALPMSPA EFEQALRAKG AYYHIHHPYH VAMYQGRATR EQIQGWVANR FYYQVNIPMK DAAILANCPD REVRREWIQR LLDHDGAPGE DGGIEAWLRL GQAVGLDPDQ LRSQELVLPG VRFAVDAYVN FARRASWQEA ASSSLTELFA PQIHQSRLDS WPQHYPWIDP AGYEYFRTRL GQARRDVEHG LAITLQHYTT RAGQERMLEI LQFKLDILWS MLDAMSMAYE LNRPPYHSVT QDRVWHKGIT L //