ID   PQQCD_METEX             Reviewed;         372 AA.
AC   Q49150; P71518;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 2.
DT   20-JAN-2009, entry version 39.
DE   RecName: Full=Bifunctional coenzyme PQQ synthesis protein C/D;
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein C/D;
DE   Includes:
DE     RecName: Full=Pyrroloquinoline-quinone synthase;
DE              EC=1.3.3.11;
DE     AltName: Full=Coenzyme PQQ synthesis protein C;
DE   Includes:
DE     RecName: Full=Coenzyme PQQ synthesis protein D;
GN   Name=pqqCD;
OS   Methylobacterium extorquens (Protomonas extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-111.
RC   STRAIN=AM1 / NCIMB 9133;
RX   MEDLINE=94179111; PubMed=8132470;
RA   Morris C.J., Biville F., Turlin E., Lee E., Ellermann K., Fan W.H.,
RA   Ramamoorthi R., Springer A.L., Lidstrom M.E.;
RT   "Isolation, phenotypic characterization, and complementation analysis
RT   of mutants of Methylobacterium extorquens AM1 unable to synthesize
RT   pyrroloquinoline quinone and sequences of pqqD, pqqG, and pqqC.";
RL   J. Bacteriol. 176:1746-1755(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-372.
RC   STRAIN=AM1 / NCIMB 9133;
RX   MEDLINE=97195805; PubMed=9043136;
RA   Toyama H., Chistoserdova L., Lidstrom M.E.;
RT   "Sequence analysis of pqq genes required for biosynthesis of
RT   pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the
RT   purification of a biosynthetic intermediate.";
RL   Microbiology 143:595-602(1997).
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: In the N-terminal section; belongs to the pqqC family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the pqqD family.
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DR   EMBL; L25889; AAA17880.1; -; Unassigned_DNA.
DR   EMBL; U72662; AAB58899.1; -; Genomic_DNA.
DR   PIR; C55527; C55527.
DR   BRENDA; 1.3.3.11; 20440.
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; fused; 1.
DR   HAMAP; MF_00655; fused; 1.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   InterPro; IPR011845; PQQ_synth_PqqC.
DR   InterPro; IPR008792; PQQ_synth_PqqD.
DR   InterPro; IPR004305; TENA/THI4/PQQ_synth_PqqC.
DR   Gene3D; G3DSA:1.20.910.10; Haem_Oase-like_multi-hlx; 1.
DR   Pfam; PF05402; PqqD; 1.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   TIGRFAMs; TIGR02111; PQQ_syn_pqqC; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; PQQ biosynthesis.
FT   CHAIN         1    372       Bifunctional coenzyme PQQ synthesis
FT                                protein C/D.
FT                                /FTId=PRO_0000219980.
FT   REGION        1    267       PqqC.
FT   REGION      268    280       Linker.
FT   REGION      281    372       PqqD.
SQ   SEQUENCE   372 AA;  41577 MW;  3E502CEB4097695D CRC64;
     MTAQFPPPVP DTEQRLLSHE ELEAALRDIG ARRYHNLHPF HRLLHDGKLS KDQVRAWALN
     RYYYQAMIPV KDAALLARLP DAQLRRIWRQ RIVDHDGDHE GDGGIERWLK LAEGVGFTRD
     YVLSTKGILS ATRFSVDAYV HFVSERSLLE AIASSLTEMF SPTIISERVA GMLKNYDFIT
     KDTLAYFDKR LTQAPRDADF ALDYVKRHAT TPEMQRAAID ALTFKCNVLW TQLDALYFAY
     VAPGMVPPDA WQPGEGLVAE TNSAEDSPAA AASPAATTAE PTAFSGSDVP RLPRGVRLRF
     DEVRNKHVLL APERTFDLDD NAVAVLKLVD GRNTVSQIAQ ILGQTYDADP AIIEADILPM
     LAGLAQKRVL ER
//