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PQQD_AZOVD
ID   PQQD_AZOVD              Reviewed;          92 AA.
AC   C1DEW6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=Avin_41650;
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303;
RX   PubMed=19429624; DOI=10.1128/jb.00504-09;
RA   Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(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; CP001157; ACO80295.1; -; Genomic_DNA.
DR   RefSeq; WP_012702667.1; NC_012560.1.
DR   AlphaFoldDB; C1DEW6; -.
DR   SMR; C1DEW6; -.
DR   STRING; 322710.Avin_41650; -.
DR   EnsemblBacteria; ACO80295; ACO80295; Avin_41650.
DR   KEGG; avn:Avin_41650; -.
DR   eggNOG; ENOG5032Z81; Bacteria.
DR   HOGENOM; CLU_163864_2_1_6; -.
DR   OMA; YVLLFPE; -.
DR   OrthoDB; 2008640at2; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000002424; 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_1000212438"
SQ   SEQUENCE   92 AA;  10482 MW;  6FB008DCFA0BD294 CRC64;
     MSETTLNDIP QLRRGFRFQW EPAQNCHVLL YPEGMVKLND SAAAILGQVD GDRSIAAIVA
     ALRERFPESD GIEEDVLEFL EVARERSWIE LH
 
 
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