ID   PQQC_GRABC              Reviewed;         255 AA.
AC   Q0BQS6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   04-NOV-2008, entry version 21.
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=GbCGDNIH1_1928;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17827295; DOI=10.1128/JB.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K.,
RA   Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W.,
RA   Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI62826.1; -; Genomic_DNA.
DR   RefSeq; YP_745749.1; -.
DR   GeneID; 4274447; -.
DR   GenomeReviews; CP000394_GR; GbCGDNIH1_1928.
DR   KEGG; gbe:GbCGDNIH1_1928; -.
DR   NMPDR; fig|391165.8.peg.1869; -.
DR   HOGENOM; Q0BQS6; -.
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    255       Pyrroloquinoline-quinone synthase.
FT                                /FTId=PRO_1000061669.
SQ   SEQUENCE   255 AA;  28760 MW;  957C05947C1C7782 CRC64;
     MTQLHNRTAG QETNRVMTPD ELEAALRAVG AERYHNLHPF HRLLHDGALT RGQVQAWALN
     RYHYQASIPA KDAALLSRLP TAELRREWRR RLVDHDGTEP GTGGIARWLK LAEGVGLDAA
     YVESREGLLP TTRFAVDAYV TFCREKPILE AIASSLTEMF SPTIIRERVS GMLANYDWVS
     EETLAYFKPR LTQAPRDVDF ALAYVKEHAR TPEQQQAVIA ALRFKCDVLW SQLDALYYSY
     VAPGNIPPGA FVPEV
//