ID   PQQC_ACIAD              Reviewed;         255 AA.
AC   Q6F9J1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   04-NOV-2008, entry version 30.
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=ACIAD2505;
OS   Acinetobacter sp. (strain ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG69273.1; -; Genomic_DNA.
DR   RefSeq; YP_047095.1; -.
DR   SMR; Q6F9J1; 5-254.
DR   GeneID; 2879637; -.
DR   GenomeReviews; CR543861_GR; ACIAD2505.
DR   KEGG; aci:ACIAD2505; -.
DR   NMPDR; fig|62977.3.peg.2104; -.
DR   HOGENOM; Q6F9J1; -.
DR   BioCyc; ASP62977:ACIAD2505-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    255       Pyrroloquinoline-quinone synthase.
FT                                /FTId=PRO_0000219975.
SQ   SEQUENCE   255 AA;  29662 MW;  B7EA183D0DF7A76A CRC64;
     MRFNMTTTLF SPAEFEQALR DKGRYYHIHH PYHIMMNDGH ATKQQIQGWV ANRFYYQVNI
     PLKDAAIMAN CPDPATRRKW VQRILDHDGQ HDDHGGIEAW LRLGEAVGLD RETILSQKMV
     LPSVRFAVDA YVNFARRACW QEAACSSLTE LFAPAIHQSR LDTWPTHYPW IDAEGYAYFR
     GRLSQANRDV EHGLELALEY CNTVDRQQRM LNILQFKLDI LWTILDGMSM AYVLERAPYH
     TVTQEAVWHQ KGLLG
//