PQQC_XANC8
ID PQQC_XANC8 Reviewed; 250 AA.
AC Q4UXI2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=XC_1171;
OS Xanthomonas campestris pv. campestris (strain 8004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=314565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8004;
RX PubMed=15899963; DOI=10.1101/gr.3378705;
RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT "Comparative and functional genomic analyses of the pathogenicity of
RT phytopathogen Xanthomonas campestris pv. campestris.";
RL Genome Res. 15:757-767(2005).
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; CP000050; AAY48241.1; -; Genomic_DNA.
DR RefSeq; WP_011038061.1; NC_007086.1.
DR AlphaFoldDB; Q4UXI2; -.
DR SMR; Q4UXI2; -.
DR EnsemblBacteria; AAY48241; AAY48241; XC_1171.
DR KEGG; xcb:XC_1171; -.
DR HOGENOM; CLU_080136_0_0_6; -.
DR OMA; AYVHFVR; -.
DR OrthoDB; 1571811at2; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000000420; 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_1000061681"
SQ SEQUENCE 250 AA; 28234 MW; DCF38F8E4F544B61 CRC64;
MTALLSPDQL EADLRAIGAR LYHDQHPFHA LLHHGKLNRG QVQAWALNRF EYQRCIPLKD
AAILARMEDP ALRRIWRQRI LDHDGNSPSD GGIARWLHLT DALGLPRELV ESGRALLPGT
RFAVQAYLHF VREKSLLEAI ASSLTELFAP NIIGQRVAGM LQHYDFVSPE ALAYFEHRLT
EAPRDSDFAL DYVKQHADTI EKQQLVKAAL HFKCSVLWAQ LDALHVAYVS PGVVWPDAFV
PERDSKRAAA