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}.
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; 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