ID   PQQC_GLUOX              Reviewed;         239 AA.
AC   Q9L3B2; Q5FS89;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 104.
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=GOX0985;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9937 / LMG 1404 / NCIMB 8084;
RX   PubMed=11111029; DOI=10.1111/j.1574-6968.2000.tb09429.x;
RA   Felder M., Gupta A., Verma V., Kumar A., Qazi G.N., Cullum J.;
RT   "The pyrroloquinoline quinone synthesis genes of Gluconobacter oxydans.";
RL   FEMS Microbiol. Lett. 193:231-236(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(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}.
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DR   EMBL; AJ277117; CAB83199.1; -; Genomic_DNA.
DR   EMBL; CP000009; AAW60757.1; -; Genomic_DNA.
DR   RefSeq; WP_011252552.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q9L3B2; -.
DR   SMR; Q9L3B2; -.
DR   STRING; 290633.GOX0985; -.
DR   EnsemblBacteria; AAW60757; AAW60757; GOX0985.
DR   KEGG; gox:GOX0985; -.
DR   eggNOG; COG5424; Bacteria.
DR   HOGENOM; CLU_080136_0_0_5; -.
DR   OMA; AYVHFVR; -.
DR   BRENDA; 1.3.3.11; 38.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000006375; 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..239
FT                   /note="Pyrroloquinoline-quinone synthase"
FT                   /id="PRO_0000219978"
FT   CONFLICT        69
FT                   /note="A -> D (in Ref. 1; CAB83199)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88..89
FT                   /note="GT -> EP (in Ref. 1; CAB83199)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   239 AA;  27293 MW;  708C883BED29C7F2 CRC64;
     MTLLTPDQLE AQLRQIGAER YHNRHPFHRK LHDGKLDKAQ VQAWALNRYY YQARIPAKDA
     TLLARLPTAE LRREWRRRIE DHDGTEPGTG GVARWLMLTD GLGLDRDYVE SLDGLLPATR
     FSVDAYVNFV RDQSILAAIA SSLTELFSPT IISERVSGML RHYDFVSEKT LAYFTPRLTQ
     APRDSDFALA YVREKARTPE QQKEVLGALE FKCSVLWTML DALDYAYVEG HIPPGAFVP