ID   PQQC_KLEPN              Reviewed;         251 AA.
AC   P27505;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 101.
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;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418;
RX   PubMed=1313537; DOI=10.1007/bf00280008;
RA   Meulenberg J.J.M., Sellink E., Riegman N.H., Postma P.W.;
RT   "Nucleotide sequence and structure of the Klebsiella pneumoniae pqq
RT   operon.";
RL   Mol. Gen. Genet. 232:284-294(1992).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418;
RX   PubMed=7665488; DOI=10.1128/jb.177.17.5088-5098.1995;
RA   Velterop J.S., Sellink E., Meulenberg J.J., David S., Bulder I.,
RA   Postma P.W.;
RT   "Synthesis of pyrroloquinoline quinone in vivo and in vitro and detection
RT   of an intermediate in the biosynthetic pathway.";
RL   J. Bacteriol. 177:5088-5098(1995).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX   PubMed=15148379; DOI=10.1073/pnas.0402640101;
RA   Magnusson O.T., Toyama H., Saeki M., Rojas A., Reed J.C., Liddington R.C.,
RA   Klinman J.P., Schwarzenbacher R.;
RT   "Quinone biogenesis: structure and mechanism of PqqC, the final catalyst in
RT   the production of pyrroloquinoline quinone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7913-7918(2004).
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:0000269|PubMed:7665488}.
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   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15148379}.
CC   -!- SIMILARITY: Belongs to the PqqC family. {ECO:0000305}.
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DR   EMBL; X58778; CAA41581.1; -; Genomic_DNA.
DR   PIR; S20455; S20455.
DR   RefSeq; WP_004225008.1; NZ_WVHM01000012.1.
DR   PDB; 1OTV; X-ray; 2.10 A; A/B=1-251.
DR   PDB; 1OTW; X-ray; 2.30 A; A/B=1-251.
DR   PDBsum; 1OTV; -.
DR   PDBsum; 1OTW; -.
DR   AlphaFoldDB; P27505; -.
DR   SMR; P27505; -.
DR   DrugBank; DB03205; Pyrroloquinoline Quinone.
DR   UCD-2DPAGE; P27505; -.
DR   BioCyc; MetaCyc:MON-15352; -.
DR   BRENDA; 1.3.3.11; 2814.
DR   UniPathway; UPA00539; -.
DR   EvolutionaryTrace; P27505; -.
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   1: Evidence at protein level;
KW   3D-structure; Oxidoreductase; PQQ biosynthesis.
FT   CHAIN           1..251
FT                   /note="Pyrroloquinoline-quinone synthase"
FT                   /id="PRO_0000219979"
FT   HELIX           9..18
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           19..22
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           24..26
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           28..34
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           40..66
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           71..85
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:1OTW"
FT   HELIX           93..103
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           108..112
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           119..134
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           137..142
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           143..149
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   TURN            162..164
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           170..181
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           189..197
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   HELIX           201..229
FT                   /evidence="ECO:0007829|PDB:1OTV"
FT   TURN            235..239
FT                   /evidence="ECO:0007829|PDB:1OTV"
SQ   SEQUENCE   251 AA;  28986 MW;  B48A494FA63B6598 CRC64;
     MLITDTLSPQ AFEEALRAKG AFYHIHHPYH IAMHNGDATR KQIQGWVANR FYYQTTIPLK
     DAAIMANCPD AQTRRKWVQR ILDHDGSHGE DGGIEAWLRL GEAVGLSRDD LLSERHVLPG
     VRFAVDAYLN FARRACWQEA ACSSLTELFA PQIHQSRLDS WPQHYPWIKE EGYFYFRSRL
     SQANRDVEHG LALAKAYCDS AEKQNRMLEI LQFKLDILWS MLDAMTMAYA LQRPPYHTVT
     DKAAWHTTRL V