ID   PQQC_XANC5              Reviewed;         250 AA.
AC   Q3BQI6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=XCV3246;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O.,
RA   Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A.,
RA   Bonas U., Bartels D., Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant
RT   pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed
RT   by the complete genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ24977.1; -; Genomic_DNA.
DR   RefSeq; YP_364977.1; -.
DR   GeneID; 3732994; -.
DR   GenomeReviews; AM039952_GR; XCV3246.
DR   KEGG; xcv:XCV3246; -.
DR   NMPDR; fig|316273.3.peg.3261; -.
DR   HOGENOM; Q3BQI6; -.
DR   OMA; Q3BQI6; AWALNRY.
DR   BioCyc; XCAM316273:XCV3246-MON; -.
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_1000061680.
SQ   SEQUENCE   250 AA;  28103 MW;  12C97099DCF08B51 CRC64;
     MTALLSPDQL EADLRAIGAR LYHDQHPFHA LLHHGKLDRG QVQAWALNRF EYQRCIPLKD
     AAILARMEDP ALRRIWRQRI LDHDGNSASD GGIARWLHLT DALGLDRTLV ESGRALLPGT
     RFAVQAYLHF VREKSLLEAI ASSLTELFAP NIIGQRVAGM LKHYDFVSSE ALAYFEHRLT
     EAPRDSDFAL DYVKQHADTV EKQALVKAAL HFKCSVLWAQ LDALHVAYVT PGIVWPDAFV
     PDRDASRVAA
//