ID   PQQC_ACIBS              Reviewed;         252 AA.
AC   B0VQD5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=ABSDF1981;
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(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; CU468230; CAP01314.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VQD5; -.
DR   SMR; B0VQD5; -.
DR   EnsemblBacteria; CAP01314; CAP01314; ABSDF1981.
DR   KEGG; abm:ABSDF1981; -.
DR   HOGENOM; CLU_080136_0_0_6; -.
DR   OMA; YYQISIP; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001741; 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..252
FT                   /note="Pyrroloquinoline-quinone synthase"
FT                   /id="PRO_1000131174"
SQ   SEQUENCE   252 AA;  29665 MW;  9D00A7DBC1CA0959 CRC64;
     MTQTPEALTT EQFKQAIIDK GQYYHIYHPF HVMMYEGKAT QQQIQAWVAN RYYYQINIPL
     KDAAIMANCP DQRVRQEWIQ RMIDQDGEYP DGGGREAWLR LAEAVGLSRE QVISEELVLP
     GVRFAVDAYV NFARRASWRE AASSSLTELF APQIHQSRLE SWPQHYPWID DKGYEYFRSR
     LSQARRDVEH GLTITLDSFT THEQQQRMLE ILQFKLDILW SILDALTLAY VHNEAPYHSV
     TQERVWHKGL FK