ID   PQQC_PSEPW              Reviewed;         251 AA.
AC   B1JDZ8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   28-JAN-2026, entry version 81.
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=PputW619_4825;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RX   PubMed=19060168; DOI=10.1128/aem.02239-08;
RA   Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N.,
RA   Barac T., Vangronsveld J., van der Lelie D.;
RT   "Genome survey and characterization of endophytic bacteria exhibiting a
RT   beneficial effect on growth and development of poplar trees.";
RL   Appl. Environ. Microbiol. 75:748-757(2009).
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; CP000949; ACA75301.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1JDZ8; -.
DR   SMR; B1JDZ8; -.
DR   STRING; 390235.PputW619_4825; -.
DR   KEGG; ppw:PputW619_4825; -.
DR   eggNOG; COG5424; Bacteria.
DR   HOGENOM; CLU_080136_0_0_6; -.
DR   OrthoDB; 9800756at2; -.
DR   UniPathway; UPA00539; -.
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.
FT   CHAIN           1..251
FT                   /note="Pyrroloquinoline-quinone synthase"
FT                   /id="PRO_1000131179"
SQ   SEQUENCE   251 AA;  29122 MW;  7934B6515C6E88BD CRC64;
     MSEALPLSPA EFEQALRAKG AYYHIHHPYH VAMYEGRATR EQIQGWVANR FYYQVNIPMK
     DAAILANCPD REVRREWIQR LLDHDGAPGE DGGIEAWLRL GQAVGLDPDQ LRSQELVLPG
     VRFAVDAYVN FARRASWQEA ASSSLTELFA PQIHQSRLDS WPQHYPWIDP AGYEYFRTRL
     GQARRDVEHG LTITLQHYTT RAAQERMLEI LQFKLDILWS MLDAMSMAYE LHRPPYHTVT
     QQRVWHKGIA L
//