ID   PQQC_CERS1              Reviewed;         255 AA.
AC   A3PMI4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   04-NOV-2026, entry version 91.
DE   RecName: Full=Pyrroloquinoline-quinone synthase {ECO:0000255|HAMAP-Rule:MF_00654};
DE            EC=1.3.3.11 {ECO:0000255|HAMAP-Rule:MF_00654};
DE   AltName: Full=Coenzyme PQQ synthesis protein C {ECO:0000255|HAMAP-Rule:MF_00654};
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein C {ECO:0000255|HAMAP-Rule:MF_00654};
GN   Name=pqqC {ECO:0000255|HAMAP-Rule:MF_00654};
GN   OrderedLocusNames=Rsph17029_2448;
OS   Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=349101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17029 / ATH 2.4.9;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ring cyclization and eight-electron oxidation of 3a-(2-amino-
CC       2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-
CC       dicarboxylic-acid to PQQ. {ECO:0000255|HAMAP-Rule:MF_00654}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-
CC         hexahydroquinoline-2,4-dicarboxylate + 3 O2 = pyrroloquinoline
CC         quinone + 2 H2O2 + 2 H2O + H(+); Xref=Rhea:RHEA:10692,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:58442, ChEBI:CHEBI:58778; EC=1.3.3.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00654};
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00654}.
CC   -!- SIMILARITY: Belongs to the PqqC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00654}.
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DR   EMBL; CP000577; ABN77550.1; -; Genomic_DNA.
DR   RefSeq; WP_011841673.1; NC_009049.1.
DR   AlphaFoldDB; A3PMI4; -.
DR   SMR; A3PMI4; -.
DR   KEGG; rsh:Rsph17029_2448; -.
DR   HOGENOM; CLU_080136_0_0_5; -.
DR   OMA; AAIMANC; -.
DR   UniPathway; UPA00539; -.
DR   GO; GO:0033732; F:pyrroloquinoline-quinone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR   HAMAP; MF_00654; PQQ_syn_PqqC; 1.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   InterPro; IPR011845; PqqC.
DR   InterPro; IPR039068; PqqC-like.
DR   InterPro; IPR004305; Thiaminase-2/PQQC.
DR   NCBIfam; TIGR02111; PQQ_syn_pqqC; 1.
DR   PANTHER; PTHR40279:SF3; 4-AMINOBENZOATE SYNTHASE; 1.
DR   PANTHER; PTHR40279; PQQC-LIKE PROTEIN; 1.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; PQQ biosynthesis.
FT   CHAIN           1..255
FT                   /note="Pyrroloquinoline-quinone synthase"
FT                   /id="PRO_1000061677"
SQ   SEQUENCE   255 AA;  29090 MW;  62D2821B96B7EF16 CRC64;
     MSLDLSTSLS PARPLESADA MEERLREIGA ARYHDRHPFH HMLHGGELTK GQVQAWALNR
     YYYQCTIPVK DAVVISRFRD RATRIEWRHR LEDHDGAEGA EGGIDRWLIL TDGLGLDRAY
     VESTDGILPA TRFAVEAYVH FVRDRSPLEA IASCLTELFA PNIHATRISG MLSHYDFINP
     TVMAYFQRRL TQAPRDADYA LRYVRDHART PEERAAVCNA LIFKTQVLWT QLDALHHAYV
     LGHVPPGAFV PEEMR
//