ID   PQQC_KLEP7              Reviewed;         251 AA.
AC   A6T9H1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=KPN78578_17810; ORFNames=KPN_01811;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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 = 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; CP000647; ABR77242.1; -; Genomic_DNA.
DR   RefSeq; WP_015958460.1; NC_009648.1.
DR   PDB; 3HLX; X-ray; 1.30 A; A/D=1-251.
DR   PDB; 3HML; X-ray; 2.35 A; A/B=1-251.
DR   PDB; 3HNH; X-ray; 1.80 A; A=1-251.
DR   PDB; 4NY7; X-ray; 1.44 A; A/B=1-251.
DR   PDBsum; 3HLX; -.
DR   PDBsum; 3HML; -.
DR   PDBsum; 3HNH; -.
DR   PDBsum; 4NY7; -.
DR   AlphaFoldDB; A6T9H1; -.
DR   SMR; A6T9H1; -.
DR   STRING; 272620.KPN_01811; -.
DR   EnsemblBacteria; ABR77242; ABR77242; KPN_01811.
DR   KEGG; kpn:KPN_01811; -.
DR   HOGENOM; CLU_080136_0_0_6; -.
DR   OMA; YYQISIP; -.
DR   BRENDA; 1.3.3.11; 2814.
DR   UniPathway; UPA00539; -.
DR   EvolutionaryTrace; A6T9H1; -.
DR   Proteomes; UP000000265; 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   1: Evidence at protein level;
KW   3D-structure; Oxidoreductase; PQQ biosynthesis; Reference proteome.
FT   CHAIN           1..251
FT                   /note="Pyrroloquinoline-quinone synthase"
FT                   /id="PRO_1000061670"
FT   HELIX           9..18
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           19..22
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           24..26
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           28..34
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           40..66
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           71..85
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           92..103
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           108..112
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:3HML"
FT   HELIX           119..134
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           137..142
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           143..148
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           150..164
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           174..197
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   HELIX           201..229
FT                   /evidence="ECO:0007829|PDB:3HLX"
FT   TURN            235..239
FT                   /evidence="ECO:0007829|PDB:3HLX"
SQ   SEQUENCE   251 AA;  29030 MW;  62122408784C8EB3 CRC64;
     MLITDTLSPQ AFEEALRAKG DFYHIHHPYH IAMHNGNATR EQIQGWVANR FYYQTTIPLK
     DAAIMANCPD AQTRRKWVQR ILDHDGSHGE DGGIEAWLRL GEAVGLSRDD LLSERHVLPG
     VRFAVDAYLN FARRACWQEA ACSSLTELFA PQIHQSRLDS WPQHYPWIKE EGYFYFRSRL
     SQANRDVEHG LALAKAYCDS AEKQNRMLEI LQFKLDILWS MLDAMTMAYA LQRPPYHTVT
     DKAAWHTTRL V