PQQC_PSEAE
ID PQQC_PSEAE Reviewed; 250 AA.
AC Q9I2C2;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=PA1987;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG05375.1; -; Genomic_DNA.
DR PIR; C83397; C83397.
DR RefSeq; NP_250677.1; NC_002516.2.
DR RefSeq; WP_003111679.1; NZ_QZGE01000026.1.
DR AlphaFoldDB; Q9I2C2; -.
DR SMR; Q9I2C2; -.
DR STRING; 287.DR97_5860; -.
DR PaxDb; Q9I2C2; -.
DR EnsemblBacteria; AAG05375; AAG05375; PA1987.
DR GeneID; 879112; -.
DR KEGG; pae:PA1987; -.
DR PATRIC; fig|208964.12.peg.2071; -.
DR PseudoCAP; PA1987; -.
DR HOGENOM; CLU_080136_0_0_6; -.
DR InParanoid; Q9I2C2; -.
DR OMA; YYQISIP; -.
DR PhylomeDB; Q9I2C2; -.
DR BioCyc; PAER208964:G1FZ6-2025-MON; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000002438; 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; Reference proteome.
FT CHAIN 1..250
FT /note="Pyrroloquinoline-quinone synthase"
FT /id="PRO_0000219982"
SQ SEQUENCE 250 AA; 29449 MW; 6245E87D0C200E46 CRC64;
MSRAAMDRAE FERALRDKGR YYHIHHPFHV AMYEGRASRE QIQGWVANRF YYQVNIPLKD
AAILANCPDR EVRREWIQRI LDHDGAPGEA GGIEAWLRLA EAVGLEREQV LSEERVLPGV
RFAVDAYVNF ARRASWQEAA SSSLTELFAP QIHQSRLDSW PRHYPWIEAA GYEYFRSRLA
QARRDVEHGL RITLEHYRTR EAQERMLDIL QFKLDVLWSM LDAMSMAYEL ERPPYHTVTR
ERVWHRGLAS