ID   PQQC_ERWT9              Reviewed;         251 AA.
AC   B2VL12;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   28-JAN-2026, entry version 82.
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=ETA_28880;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(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 = pyrroloquinoline
CC         quinone + 2 H2O2 + 2 H2O + H(+); Xref=Rhea:RHEA:10692,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, 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; CU468135; CAO97934.1; -; Genomic_DNA.
DR   RefSeq; WP_012442589.1; NC_010694.1.
DR   AlphaFoldDB; B2VL12; -.
DR   SMR; B2VL12; -.
DR   STRING; 465817.ETA_28880; -.
DR   KEGG; eta:ETA_28880; -.
DR   eggNOG; COG5424; Bacteria.
DR   HOGENOM; CLU_080136_0_0_6; -.
DR   OrthoDB; 9800756at2; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001726; Chromosome.
DR   GO; GO:0033732; F:pyrroloquinoline-quinone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd19370; TenA_PqqC; 1.
DR   Gene3D; 1.20.910.10; Heme oxygenase-like; 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   NCBIfam; TIGR02111; PQQ_syn_pqqC; 1.
DR   PANTHER; PTHR40279:SF3; 4-AMINOBENZOATE SYNTHASE; 1.
DR   PANTHER; PTHR40279; PQQC-LIKE PROTEIN; 1.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; PQQ biosynthesis; Reference proteome.
FT   CHAIN           1..251
FT                   /note="Pyrroloquinoline-quinone synthase"
FT                   /id="PRO_1000131176"
SQ   SEQUENCE   251 AA;  29088 MW;  3ED600C541DBEDC7 CRC64;
     MTEPALMTPQ QFEQALRARG AYYHIYHPYH IAMHNGEATR EQIQGWVANR FYYQTRIPLK
     DAAIMANCPD AATRRKWVQR ILDHDGHDDS DGGIEAWLRL GEAVGLDREV LLSEQLVLPG
     VRFAVDAYVS FARRAVWQEA ACSSLTELFA PEIHQSRLDS WPQHYPWIEE EGYGYFRGRL
     GQARRDVEHG LQLALAYCNS VEKQQRMLEI LQFKLDILWS MLDAMTMAYT LNRAPYHTVT
     DQPVWHQGKL L
//