PQQC_XANAC
ID PQQC_XANAC Reviewed; 250 AA.
AC Q8PHY3;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=XAC3115;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008923; AAM37960.1; -; Genomic_DNA.
DR RefSeq; WP_011052046.1; NC_003919.1.
DR AlphaFoldDB; Q8PHY3; -.
DR SMR; Q8PHY3; -.
DR STRING; 190486.XAC3115; -.
DR EnsemblBacteria; AAM37960; AAM37960; XAC3115.
DR GeneID; 66912182; -.
DR KEGG; xac:XAC3115; -.
DR eggNOG; COG5424; Bacteria.
DR HOGENOM; CLU_080136_0_0_6; -.
DR OMA; AYVHFVR; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000000576; 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_0000219989"
SQ SEQUENCE 250 AA; 28043 MW; 4B097099C15C8D8A CRC64;
MTALLGPDQL EADLRAIGAR LYHDQHPFHA LLHHGKLDRG QVQAWALNRF EYQRCIPLKD
AAILARMEDP ALRRIWRQRI LDHDGNSASD GGIARWLHLT DALGLDRTLV ESGRALLPGT
RFAVQAYLHF VREKSLLEAI ASSLTELFAP NIIGQRVAGM LKHYDFVSSE ALAYFEHRLT
EAPRDSDFAL DYVKQHADTV EKQALVKAAL HFKCSVLWAQ LDALHVAYVA PGIVWPDAFV
PDRDASRVAA