ID   PQQD_XANCB              Reviewed;          92 AA.
AC   B0RQ26;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
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};
GN   OrderedLocusNames=xcc-b100_1213;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP50561.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RQ26; -.
DR   SMR; B0RQ26; -.
DR   KEGG; xca:xcc-b100_1213; -.
DR   HOGENOM; CLU_163864_0_0_6; -.
DR   OMA; WVILAPE; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001188; 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..92
FT                   /note="PqqA binding protein"
FT                   /id="PRO_1000131192"
SQ   SEQUENCE   92 AA;  10331 MW;  141C4597E0418F64 CRC64;
     MSTISRDSCP ALRAGVRLQH DRARDQWVLL APERVVELDD IALVVAQRYD GTQSLAEIAQ
     TLATEFDADA SEIETDVIEL TTTLHQKRLL RL