ID   B2AIN6_CUPTR            Unreviewed;       252 AA.
AC   B2AIN6;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   04-NOV-2026, entry version 100.
DE   RecName: Full=Pyrroloquinoline-quinone synthase {ECO:0000256|HAMAP-Rule:MF_00654};
DE            EC=1.3.3.11 {ECO:0000256|HAMAP-Rule:MF_00654};
DE   AltName: Full=Coenzyme PQQ synthesis protein C {ECO:0000256|HAMAP-Rule:MF_00654};
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein C {ECO:0000256|HAMAP-Rule:MF_00654};
GN   Name=pqqC2 {ECO:0000313|EMBL:CAP63635.1};
GN   Synonyms=pqqC {ECO:0000256|HAMAP-Rule:MF_00654};
GN   OrderedLocusNames=RALTA_B0440 {ECO:0000313|EMBL:CAP63635.1};
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880 {ECO:0000313|EMBL:CAP63635.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAP63635.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(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:0000256|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:0000256|HAMAP-Rule:MF_00654};
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00654}.
CC   -!- SIMILARITY: Belongs to the PqqC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00654}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU633750; CAP63635.1; -; Genomic_DNA.
DR   RefSeq; WP_012355288.1; NC_010530.1.
DR   AlphaFoldDB; B2AIN6; -.
DR   GeneID; 29764715; -.
DR   KEGG; cti:RALTA_B0440; -.
DR   eggNOG; COG5424; Bacteria.
DR   HOGENOM; CLU_080136_0_0_4; -.
DR   OMA; AANCFYY; -.
DR   BioCyc; CTAI977880:RALTA_RS17880-MONOMER; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001692; Chromosome 2.
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   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 {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00654};
KW   PQQ biosynthesis {ECO:0000256|ARBA:ARBA00022905, ECO:0000256|HAMAP-
KW   Rule:MF_00654}; Reference proteome {ECO:0000313|Proteomes:UP000001692}.
FT   DOMAIN          18..226
FT                   /note="Thiaminase-2/PQQC"
FT                   /evidence="ECO:0000259|Pfam:PF03070"
SQ   SEQUENCE   252 AA;  28464 MW;  223CDEE86FF91BB6 CRC64;
     MNNPSTGVLS PAELEGALRK IGHERYHNRH PFHRLLHTGA LTLGQVQAWA LNRYCYQAAI
     PRKDAALISR VTDRSLRREW VHRILDHDGW GEKEGGIDRW LVLTDSLGLD RDYVVSQRGV
     LPATVFAVEA YVDFVARHSP VVAVASCLTE LFAPDIHRER IAGMLENYPF ISESVLVYFR
     RRLDQAPRDA EFALDYVKRN ARTQSEQQGV LDALTFKCNV LWAQLDALYA AYVSPGTIPP
     GAFDPSELPC LR
//