ID   PQQC_RHIME              Reviewed;         256 AA.
AC   Q9EXV0;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
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}; OrderedLocusNames=RB0199;
GN   ORFNames=SMb20206;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymB (megaplasmid 2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1021;
RA   Finan T.M., Aneja P., Chain P., Napper K., Golding B.;
RT   "Mineral phosphate solubilization in Sinorhizobium meliloti.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481431; DOI=10.1073/pnas.161294698;
RA   Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA   Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT   "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT   endosymbiont Sinorhizobium meliloti.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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; AL591985; CAC48599.1; -; Genomic_DNA.
DR   PIR; G95866; G95866.
DR   RefSeq; NP_436739.1; NC_003078.1.
DR   RefSeq; WP_010975104.1; NC_003078.1.
DR   AlphaFoldDB; Q9EXV0; -.
DR   SMR; Q9EXV0; -.
DR   STRING; 266834.SM_b20206; -.
DR   EnsemblBacteria; CAC48599; CAC48599; SM_b20206.
DR   GeneID; 61600214; -.
DR   KEGG; sme:SM_b20206; -.
DR   PATRIC; fig|266834.11.peg.5115; -.
DR   eggNOG; COG5424; Bacteria.
DR   HOGENOM; CLU_080136_0_0_5; -.
DR   OMA; AYVHFVR; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001976; Plasmid pSymB.
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   3: Inferred from homology;
KW   Oxidoreductase; Plasmid; PQQ biosynthesis; Reference proteome.
FT   CHAIN           1..256
FT                   /note="Pyrroloquinoline-quinone synthase"
FT                   /id="PRO_0000219986"
SQ   SEQUENCE   256 AA;  28818 MW;  5693DC9037E5E304 CRC64;
     MTTATDRQAF HARLLEIGKE RYHDKHPFHA MLHGGGCTTT QVRAWVINRY YYQSRIPMKD
     AAFLSRCDDP DMRRAWRSRI EDHDGGVEEG GGIRRWLRLA EAVGLDPAYV GSARGVLPST
     RFAVDAYVSF VREKPLLEAV ASSLTELFAP KIHSERIAGL LEHYAFADDA ALAYFRQRLA
     EVPRDVEFGL AYVLDHADTR EKQDAAAQAL TFKTDVLWAQ LDALYSAYVT PGRIPPGAWD
     GREGVIREPR AREAAE