ID   PQQD_RUEPO              Reviewed;          95 AA.
AC   Q5LTB3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=SPO1501;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000031; AAV94788.1; -; Genomic_DNA.
DR   RefSeq; WP_011047238.1; NC_003911.12.
DR   AlphaFoldDB; Q5LTB3; -.
DR   SMR; Q5LTB3; -.
DR   STRING; 246200.SPO1501; -.
DR   EnsemblBacteria; AAV94788; AAV94788; SPO1501.
DR   KEGG; sil:SPO1501; -.
DR   eggNOG; COG0535; Bacteria.
DR   HOGENOM; CLU_163864_0_0_5; -.
DR   OMA; KHVRIQY; -.
DR   OrthoDB; 2008640at2; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001023; 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; Reference proteome.
FT   CHAIN           1..95
FT                   /note="PqqA binding protein"
FT                   /id="PRO_0000219972"
SQ   SEQUENCE   95 AA;  10299 MW;  78885330CFFF6F49 CRC64;
     MTLALAPTDR PYLPRGVRLV TDRVRGGIVL LAPEKAVALD AVGEAILSRV DGQTSLAALV
     DQLVEAYDAP REQIEQDVQA FLQGLRARMF LMVAP