PQQD_XANCP
ID PQQD_XANCP Reviewed; 92 AA.
AC Q8P6M8;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=XCC2939;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008922; AAM42211.1; -; Genomic_DNA.
DR RefSeq; NP_638287.1; NC_003902.1.
DR RefSeq; WP_011038062.1; NC_003902.1.
DR PDB; 3G2B; X-ray; 1.66 A; A=1-92.
DR PDBsum; 3G2B; -.
DR AlphaFoldDB; Q8P6M8; -.
DR SMR; Q8P6M8; -.
DR STRING; 340.xcc-b100_1213; -.
DR EnsemblBacteria; AAM42211; AAM42211; XCC2939.
DR KEGG; xcc:XCC2939; -.
DR PATRIC; fig|190485.4.peg.3143; -.
DR eggNOG; COG0535; Bacteria.
DR HOGENOM; CLU_163864_0_0_6; -.
DR OMA; WVILAPE; -.
DR UniPathway; UPA00539; -.
DR EvolutionaryTrace; Q8P6M8; -.
DR Proteomes; UP000001010; 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 1: Evidence at protein level;
KW 3D-structure; PQQ biosynthesis; Reference proteome.
FT CHAIN 1..92
FT /note="PqqA binding protein"
FT /id="PRO_0000219974"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:3G2B"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:3G2B"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:3G2B"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:3G2B"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3G2B"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:3G2B"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:3G2B"
SQ SEQUENCE 92 AA; 10300 MW; 141C458BE9D10A64 CRC64;
MSTISRDSCP ALRAGVRLQH DRARDQWVLL APERVVELDD IALVVAQRYD GTQSLAQIAQ
TLAAEFDADA SEIETDVIEL TTTLHQKRLL RL