PQQC_XANOP
ID PQQC_XANOP Reviewed; 250 AA.
AC B2SSW1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=PXO_01590;
OS Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=360094;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PXO99A;
RX PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA White F.F., Bogdanove A.J.;
RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT oryzae pv. oryzae PXO99A.";
RL BMC Genomics 9:204-204(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 = 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; CP000967; ACD59800.1; -; Genomic_DNA.
DR RefSeq; WP_012445333.1; NC_010717.2.
DR AlphaFoldDB; B2SSW1; -.
DR SMR; B2SSW1; -.
DR STRING; 360094.PXO_01590; -.
DR EnsemblBacteria; ACD59800; ACD59800; PXO_01590.
DR KEGG; xop:PXO_01590; -.
DR eggNOG; COG5424; Bacteria.
DR HOGENOM; CLU_080136_0_0_6; -.
DR OMA; AYVHFVR; -.
DR OrthoDB; 1571811at2; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000001740; Chromosome.
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; PQQ biosynthesis.
FT CHAIN 1..250
FT /note="Pyrroloquinoline-quinone synthase"
FT /id="PRO_1000131182"
SQ SEQUENCE 250 AA; 28027 MW; 42C8FD997A4AE2E6 CRC64;
MSALLSPDQL EADLRAIGAR LYHDQHPFHA LLHHGKLDRG QVQAWALNRF EYQRCIPLKD
AAILARMEDP ALRRIWRQRI VDHDGNSTTD GGIARWLHLT DALGLDRTLV ESGRALLPGT
RFAVQAYLQF VSEKSLLEAI ASSLTELFAP NIIGQRVAGM LKHYDFVSSD ALAYFEHRLT
EAPRDSDFAL DYVKQHADTV EKQALVKAAL HFKCSVLWAQ LDALHVAYVT PGIVWPDAFV
PDRDASRVAA