ID   PQQC_XANOR              Reviewed;         250 AA.
AC   Q5H233;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 88.
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}; OrderedLocusNames=XOO1734;
OS   Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC10331 / KXO85;
RX   PubMed=15673718; DOI=10.1093/nar/gki206;
RA   Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA   Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA   Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA   Go S.-J.;
RT   "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT   bacterial blight pathogen of rice.";
RL   Nucleic Acids Res. 33:577-586(2005).
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 = H(+) + 2 H2O + 2 H2O2 +
CC         pyrroloquinoline quinone; Xref=Rhea:RHEA:10692, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW74988.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE013598; AAW74988.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041182064.1; NC_006834.1.
DR   AlphaFoldDB; Q5H233; -.
DR   SMR; Q5H233; -.
DR   STRING; 291331.XOO1734; -.
DR   EnsemblBacteria; AAW74988; AAW74988; XOO1734.
DR   KEGG; xoo:XOO1734; -.
DR   PATRIC; fig|291331.8.peg.1933; -.
DR   HOGENOM; CLU_080136_0_0_6; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000006735; Chromosome.
DR   GO; GO:0033732; F:pyrroloquinoline-quinone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:UniProt.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.910.10; -; 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   PANTHER; PTHR40279; PTHR40279; 1.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   SUPFAM; SSF48613; SSF48613; 1.
DR   TIGRFAMs; TIGR02111; PQQ_syn_pqqC; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; PQQ biosynthesis; Reference proteome.
FT   CHAIN           1..250
FT                   /note="Pyrroloquinoline-quinone synthase"
FT                   /id="PRO_0000219991"
SQ   SEQUENCE   250 AA;  27997 MW;  53C8F13EBC9D3996 CRC64;
     MSALLSPDQL EADLRAIGAR LYHDQHPFHA LLHHGKLDRG QVQAWALNRF EYQRCIPLKD
     AAILARMEDP ALRRIWRQRI VDHDGNSATD GGIARWLHLT DALGLDRTLV ESGRALLPGT
     RFAVQAYLQF VSEKSLLEAI ASSLTELFAP NIIGQRVAGM LKHYDFVSSD ALAYFEHRLT
     EAPRDSDFAL DYVKQHADTV EKQALVKAAL HFKCSVLWAQ LDALHVAYVT PGIVWPDAFV
     PDRDASRVAA