ID   B1ZIB3_METPB            Unreviewed;       362 AA.
AC   B1ZIB3;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   04-NOV-2026, entry version 108.
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=pqqC {ECO:0000256|HAMAP-Rule:MF_00654};
GN   OrderedLocusNames=Mpop_1770 {ECO:0000313|EMBL:ACB79933.1};
OS   Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS   (Methylobacterium populi).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=441620 {ECO:0000313|EMBL:ACB79933.1, ECO:0000313|Proteomes:UP000007136};
RN   [1] {ECO:0000313|EMBL:ACB79933.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJ001 {ECO:0000313|EMBL:ACB79933.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL   Submitted (APR-2008) 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: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|ARBA:ARBA00004886, ECO:0000256|HAMAP-Rule:MF_00654}.
CC   -!- SUBUNIT: Monomer. Interacts with PqqE. {ECO:0000256|ARBA:ARBA00011741}.
CC   -!- SIMILARITY: Belongs to the PqqC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00654}.
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DR   EMBL; CP001029; ACB79933.1; -; Genomic_DNA.
DR   RefSeq; WP_012453679.1; NC_010725.1.
DR   STRING; 441620.Mpop_1770; -.
DR   GeneID; 31775939; -.
DR   KEGG; mpo:Mpop_1770; -.
DR   eggNOG; COG0535; Bacteria.
DR   eggNOG; COG5424; Bacteria.
DR   HOGENOM; CLU_764642_0_0_5; -.
DR   OMA; AAIMANC; -.
DR   OrthoDB; 9800756at2; -.
DR   UniPathway; UPA00539; -.
DR   CDD; cd19370; TenA_PqqC; 1.
DR   Gene3D; 1.10.10.1150; Coenzyme PQQ synthesis protein D (PqqD); 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; IPR008792; PQQD.
DR   InterPro; IPR022479; PqqD_bac.
DR   InterPro; IPR041881; PqqD_sf.
DR   InterPro; IPR004305; Thiaminase-2/PQQC.
DR   PANTHER; PTHR40279:SF3; 4-AMINOBENZOATE SYNTHASE; 1.
DR   PANTHER; PTHR40279; PQQC-LIKE PROTEIN; 1.
DR   Pfam; PF05402; PqqD; 1.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR   NCBIfam; TIGR03859; PQQ_PqqD; 1.
DR   NCBIfam; TIGR02111; PQQ_syn_pqqC; 1.
DR   GO; GO:0033732; F:pyrroloquinoline-quinone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Proteomes; UP000007136; Chromosome.
DR   AlphaFoldDB; B1ZIB3; -.
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:UP000007136}.
FT   DOMAIN          24..234
FT                   /note="Thiaminase-2/PQQC"
FT                   /evidence="ECO:0000259|Pfam:PF03070"
SQ   SEQUENCE   362 AA;  40432 MW;  166DA9836D046F4A CRC64;
     MTAQFPPPVP EAEQRLLSHE ELEAALRDIG ARRYHNLHPF HRLLHDGKLS KDQVRAWALN
     RYYYQAMIPV KDAALLARLP DAQLRRIWRQ RIVDHDGDHE GDGGIERWLK LAEGVGFARD
     YVLSTKGILS ATRFSVDAYV HFVSERTLLE AIASSLTEMF SPTIISERVA GMLKNYDFIT
     KETLAYFDKR LTQAPRDADF ALDYVKRHAT TPEMQRAAME ALTFKCNVLW TQLDALYFAY
     VAPGMIPPDA WQPGEGLVAE GAPAAATAGA PAAFSGSDVP RLPRGVRLRY DEVRAKHVLL
     APERTFDLDD NAVAVLKLVD GQNSVSQIAR TLGQTYDADP AVIEADILPM LAGLAQKRVL
     ER
//