ID   PQQC_XANCB              Reviewed;         250 AA.
AC   B0RQ27;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=xcc-b100_1214;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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}.
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DR   EMBL; AM920689; CAP50562.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RQ27; -.
DR   SMR; B0RQ27; -.
DR   KEGG; xca:xcc-b100_1214; -.
DR   HOGENOM; CLU_080136_0_0_6; -.
DR   OMA; AYVHFVR; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001188; 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.
FT   CHAIN           1..250
FT                   /note="Pyrroloquinoline-quinone synthase"
FT                   /id="PRO_1000131181"
SQ   SEQUENCE   250 AA;  28235 MW;  8C5785CEE83EEBC6 CRC64;
     MTALLSPDQL EADLRAIGAR LYHDQHPFHA LLHHGKLDRG QVQAWALNRF EYQRCIPLKD
     AAILARMEDP ALRRIWRQRI LDHDGNSPSD GGIARWLHLT DALGLPRELV ESGRALLPGT
     RFAVQAYLHF VREKSLLEAI ASSLTELFAP NIIGQRVAGM LQHYDFVSPE ALAYFEHRLT
     EAPRDSDFAL DYVKQHADTI EKQQLVKAAL HFKCSVLWAQ LDALHVAYVS PGVVWPDAFV
     PERDSKRAAA