ID   PQQD_KLEPN              Reviewed;          92 AA.
AC   P27506;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 81.
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;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418;
RX   PubMed=1313537; DOI=10.1007/bf00280008;
RA   Meulenberg J.J.M., Sellink E., Riegman N.H., Postma P.W.;
RT   "Nucleotide sequence and structure of the Klebsiella pneumoniae pqq
RT   operon.";
RL   Mol. Gen. Genet. 232:284-294(1992).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418;
RX   PubMed=7665488; DOI=10.1128/jb.177.17.5088-5098.1995;
RA   Velterop J.S., Sellink E., Meulenberg J.J., David S., Bulder I.,
RA   Postma P.W.;
RT   "Synthesis of pyrroloquinoline quinone in vivo and in vitro and detection
RT   of an intermediate in the biosynthetic pathway.";
RL   J. Bacteriol. 177:5088-5098(1995).
RN   [3]
RP   INTERACTION WITH PQQE.
RX   PubMed=20737074; DOI=10.1039/c0cc00968g;
RA   Wecksler S.R., Stoll S., Iavarone A.T., Imsand E.M., Tran H., Britt R.D.,
RA   Klinman J.P.;
RT   "Interaction of PqqE and PqqD in the pyrroloquinoline quinone (PQQ)
RT   biosynthetic pathway links PqqD to the radical SAM superfamily.";
RL   Chem. Commun. (Camb.) 46:7031-7033(2010).
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:0000269|PubMed:20737074}.
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; X58778; CAA41582.1; -; Genomic_DNA.
DR   PIR; S20456; S20456.
DR   RefSeq; WP_004143686.1; NZ_WYAM01000001.1.
DR   AlphaFoldDB; P27506; -.
DR   SMR; P27506; -.
DR   UniPathway; UPA00539; -.
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   1: Evidence at protein level;
KW   PQQ biosynthesis.
FT   CHAIN           1..92
FT                   /note="PqqA binding protein"
FT                   /id="PRO_0000219963"
SQ   SEQUENCE   92 AA;  10436 MW;  8439A81EC13BC8A1 CRC64;
     MQKTSIVAFR RGYRLQWEAA QESHVILYPE GMAKLNETAA AILELVDGRR DVAAIIAMLN
     ERFPEAGGVD DDVIEFLQIA CQQKWITCRE PE