ID   PQQC_PSEU2              Reviewed;         251 AA.
AC   Q4ZMC3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Pyrroloquinoline-quinone synthase;
DE            EC=1.3.3.11;
DE   AltName: Full=Coenzyme PQQ synthesis protein C;
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein C;
GN   Name=pqqC; OrderedLocusNames=Psyr_4672;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Ring cyclization and eight-electron oxidation of 3a-(2-
CC       amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-
CC       7,9-dicarboxylic-acid to PQQ (By similarity).
CC   -!- CATALYTIC ACTIVITY: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-
CC       1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O(2) = 4,5-
CC       dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate
CC       + 2 H(2)O(2) + 2 H(2)O.
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the pqqC family.
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DR   EMBL; CP000075; AAY39699.1; -; Genomic_DNA.
DR   RefSeq; YP_237737.1; -.
DR   SMR; Q4ZMC3; 7-246.
DR   GeneID; 3370222; -.
DR   GenomeReviews; CP000075_GR; Psyr_4672.
DR   KEGG; psb:Psyr_4672; -.
DR   NMPDR; fig|205918.4.peg.3735; -.
DR   HOGENOM; Q4ZMC3; -.
DR   OMA; Q4ZMC3; DSWPQHY.
DR   BioCyc; PSYR205918:PSYR_4672-MON; -.
DR   GO; GO:0033732; F:pyrroloquinoline-quinone synthase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00654; -; 1.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   InterPro; IPR011845; PQQ_synth_PqqC.
DR   InterPro; IPR004305; TENA/THI4/PQQ_synth_PqqC.
DR   Gene3D; G3DSA:1.20.910.10; Haem_Oase-like_multi-hlx; 1.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   TIGRFAMs; TIGR02111; PQQ_syn_pqqC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Oxidoreductase; PQQ biosynthesis.
FT   CHAIN         1    251       Pyrroloquinoline-quinone synthase.
FT                                /FTId=PRO_1000061676.
SQ   SEQUENCE   251 AA;  29117 MW;  E5FCA799BA306006 CRC64;
     MSEATALSPA EFEQALRAKG AYYHIYHPFH VAMYEGRATR EQIQGWVANR FYYQVNIPLK
     DAAILANCPD REIRREWIQR LLDHDGAPGE DGGIEAWLRL GQAVGLDPDQ LRSQELVLPG
     VRFAVDAYVN FARRANWQEA ASSSLTELFA PQIHQSRLDS WPQHYPWIDP AGYEYFRTRL
     GQARRDVEHG LAITLQHYTT YEGQQRMLEI LQFKLDILWS MLDAMSMAYE LNRPPYHSVT
     DQRVWHKGIT L
//