GenomeNet

Database: UniProt
Entry: PQQD_RHOP2
LinkDB: PQQD_RHOP2
Original site: PQQD_RHOP2 
ID   PQQD_RHOP2              Reviewed;         102 AA.
AC   Q2IUJ4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=RPB_3420;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000250; ABD08116.1; -; Genomic_DNA.
DR   RefSeq; WP_011442300.1; NC_007778.1.
DR   AlphaFoldDB; Q2IUJ4; -.
DR   SMR; Q2IUJ4; -.
DR   STRING; 316058.RPB_3420; -.
DR   KEGG; rpb:RPB_3420; -.
DR   eggNOG; COG0535; Bacteria.
DR   HOGENOM; CLU_163864_0_0_5; -.
DR   OrthoDB; 7995890at2; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000008809; 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; 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.
FT   CHAIN           1..102
FT                   /note="PqqA binding protein"
FT                   /id="PRO_1000061691"
SQ   SEQUENCE   102 AA;  11368 MW;  6532A3246FDAFE86 CRC64;
     MASRHISVSE QSRPMLPRHA KLRFDETRQR WVILAPERVL APDDIAVEIL QLCDGARSVA
     AIIDTLALKY TADRAEIGAD VIAMLQDLAD KGFLTEAREK TP
//
DBGET integrated database retrieval system