ID PQQC_XANAC Reviewed; 250 AA. AC Q8PHY3; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 38. 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=XAC3115; OS Xanthomonas axonopodis pv. citri (Citrus canker). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=92829; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). 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; AE011955; AAM37960.1; -; Genomic_DNA. DR RefSeq; NP_643424.1; -. DR GeneID; 1157186; -. DR GenomeReviews; AE008923_GR; XAC3115. DR KEGG; xac:XAC3115; -. DR NMPDR; fig|190486.1.peg.3068; -. DR HOGENOM; Q8PHY3; -. DR OMA; Q8PHY3; AWALNRY. DR BioCyc; XAXO190486:XAC3115-MON; -. DR BRENDA; 1.3.3.11; 289771. 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 1 250 Pyrroloquinoline-quinone synthase. FT /FTId=PRO_0000219989. SQ SEQUENCE 250 AA; 28043 MW; 4B097099C15C8D8A CRC64; MTALLGPDQL EADLRAIGAR LYHDQHPFHA LLHHGKLDRG QVQAWALNRF EYQRCIPLKD AAILARMEDP ALRRIWRQRI LDHDGNSASD GGIARWLHLT DALGLDRTLV ESGRALLPGT RFAVQAYLHF VREKSLLEAI ASSLTELFAP NIIGQRVAGM LKHYDFVSSE ALAYFEHRLT EAPRDSDFAL DYVKQHADTV EKQALVKAAL HFKCSVLWAQ LDALHVAYVA PGIVWPDAFV PDRDASRVAA //