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PQQD_PSEPF
ID   PQQD_PSEPF              Reviewed;          91 AA.
AC   Q3K5Q7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=PqqA binding protein {ECO:0000255|HAMAP-Rule:MF_00655};
DE   AltName: Full=Coenzyme PQQ synthesis protein D {ECO:0000255|HAMAP-Rule:MF_00655};
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein D {ECO:0000255|HAMAP-Rule:MF_00655};
GN   Name=pqqD {ECO:0000255|HAMAP-Rule:MF_00655}; OrderedLocusNames=Pfl01_5160;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Functions as a PqqA binding protein and presents PqqA to
CC       PqqE, in the pyrroloquinoline quinone (PQQ) biosynthetic pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_00655}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00655}.
CC   -!- SUBUNIT: Monomer. Interacts with PqqE. {ECO:0000255|HAMAP-
CC       Rule:MF_00655}.
CC   -!- SIMILARITY: Belongs to the PqqD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00655}.
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DR   EMBL; CP000094; ABA76897.1; -; Genomic_DNA.
DR   RefSeq; WP_011336229.1; NC_007492.2.
DR   AlphaFoldDB; Q3K5Q7; -.
DR   SMR; Q3K5Q7; -.
DR   STRING; 205922.Pfl01_5160; -.
DR   EnsemblBacteria; ABA76897; ABA76897; Pfl01_5160.
DR   KEGG; pfo:Pfl01_5160; -.
DR   eggNOG; ENOG5032Z81; Bacteria.
DR   HOGENOM; CLU_163864_2_1_6; -.
DR   OMA; YVLLFPE; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.1150; -; 1.
DR   HAMAP; MF_00655; PQQ_syn_PqqD; 1.
DR   InterPro; IPR008792; PQQD.
DR   InterPro; IPR022479; PqqD_bac.
DR   InterPro; IPR041881; PqqD_sf.
DR   Pfam; PF05402; PqqD; 1.
DR   TIGRFAMs; TIGR03859; PQQ_PqqD; 1.
PE   3: Inferred from homology;
KW   PQQ biosynthesis.
FT   CHAIN           1..91
FT                   /note="PqqA binding protein"
FT                   /id="PRO_1000061688"
SQ   SEQUENCE   91 AA;  10290 MW;  5AD843EA201E4214 CRC64;
     MSFDRSKTPT WRPGYRFQYE PAQKGHVLLY PEGMIKLNES AALIGGLIDG ERDVAAIIAE
     LDKQFPGVPE LGDDIEQFME VARAQHWITL D
 
 
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