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Database: UniProt
Entry: E7PF14_PSESG
LinkDB: E7PF14_PSESG
Original site: E7PF14_PSESG 
ID   E7PF14_PSESG            Unreviewed;        94 AA.
AC   E7PF14;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=PqqA binding protein {ECO:0000256|HAMAP-Rule:MF_00655};
DE   AltName: Full=Coenzyme PQQ synthesis protein D {ECO:0000256|HAMAP-Rule:MF_00655};
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein D {ECO:0000256|HAMAP-Rule:MF_00655};
GN   Name=pqqD {ECO:0000256|HAMAP-Rule:MF_00655};
GN   ORFNames=Pgy4_02110 {ECO:0000313|EMBL:EGH06458.1};
OS   Pseudomonas savastanoi pv. glycinea str. race 4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=875330 {ECO:0000313|EMBL:EGH06458.1, ECO:0000313|Proteomes:UP000005466};
RN   [1] {ECO:0000313|EMBL:EGH06458.1, ECO:0000313|Proteomes:UP000005466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000005466};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
CC   -!- FUNCTION: Functions as a PqqA binding protein and presents PqqA to
CC       PqqE, in the pyrroloquinoline quinone (PQQ) biosynthetic pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_00655}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004886, ECO:0000256|HAMAP-Rule:MF_00655}.
CC   -!- SUBUNIT: Monomer. Interacts with PqqE. {ECO:0000256|ARBA:ARBA00011741,
CC       ECO:0000256|HAMAP-Rule:MF_00655}.
CC   -!- SIMILARITY: Belongs to the PqqD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00655}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGH06458.1}.
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DR   EMBL; ADWY01000094; EGH06458.1; -; Genomic_DNA.
DR   RefSeq; WP_004654744.1; NZ_AEGH01000003.1.
DR   AlphaFoldDB; E7PF14; -.
DR   SMR; E7PF14; -.
DR   PATRIC; fig|875330.5.peg.158; -.
DR   HOGENOM; CLU_163864_2_1_6; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000005466; Unassembled WGS sequence.
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; Coenzyme PQQ synthesis protein D (PqqD); 1.
DR   HAMAP; MF_00655; PQQ_syn_PqqD; 1.
DR   InterPro; IPR008792; PQQD.
DR   InterPro; IPR022479; PqqD_bac.
DR   InterPro; IPR041881; PqqD_sf.
DR   NCBIfam; TIGR03859; PQQ_PqqD; 1.
DR   Pfam; PF05402; PqqD; 1.
PE   3: Inferred from homology;
KW   PQQ biosynthesis {ECO:0000256|ARBA:ARBA00022905, ECO:0000256|HAMAP-
KW   Rule:MF_00655}.
SQ   SEQUENCE   94 AA;  10834 MW;  D84CCD8AB5A053E6 CRC64;
     MKHDPQFRAL TPKWHQGYRF QYEPAQKAHV VLYPEGMIKL NDSAALIGGL IDGKRTITAI
     IHELQQQFPN VPELGMDVDE FMEGTKKKNW IDLV
//
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