PQQE_PSEF5
ID PQQE_PSEF5 Reviewed; 389 AA.
AC Q4K4U8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=PqqA peptide cyclase {ECO:0000255|HAMAP-Rule:MF_00660};
DE EC=1.21.98.4 {ECO:0000255|HAMAP-Rule:MF_00660};
DE AltName: Full=Coenzyme PQQ synthesis protein E {ECO:0000255|HAMAP-Rule:MF_00660};
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein E {ECO:0000255|HAMAP-Rule:MF_00660};
GN Name=pqqE {ECO:0000255|HAMAP-Rule:MF_00660}; OrderedLocusNames=PFL_5677;
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
CC -!- FUNCTION: Catalyzes the cross-linking of a glutamate residue and a
CC tyrosine residue in the PqqA protein as part of the biosynthesis of
CC pyrroloquinoline quinone (PQQ). {ECO:0000255|HAMAP-Rule:MF_00660}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[PQQ precursor protein] + S-adenosyl-L-methionine = 5'-
CC deoxyadenosine + E-Y cross-linked-[PQQ precursor protein] + H(+) + L-
CC methionine; Xref=Rhea:RHEA:56836, Rhea:RHEA-COMP:14800, Rhea:RHEA-
CC COMP:14801, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:141026, ChEBI:CHEBI:141027;
CC EC=1.21.98.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00660};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00660};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|HAMAP-Rule:MF_00660};
CC -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00660}.
CC -!- SUBUNIT: Interacts with PqqD. The interaction is necessary for activity
CC of PqqE. {ECO:0000255|HAMAP-Rule:MF_00660}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. PqqE family.
CC {ECO:0000255|HAMAP-Rule:MF_00660}.
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DR EMBL; CP000076; AAY94867.1; -; Genomic_DNA.
DR RefSeq; WP_011063852.1; NC_004129.6.
DR AlphaFoldDB; Q4K4U8; -.
DR SMR; Q4K4U8; -.
DR STRING; 220664.PFL_5677; -.
DR EnsemblBacteria; AAY94867; AAY94867; PFL_5677.
DR KEGG; pfl:PFL_5677; -.
DR PATRIC; fig|220664.5.peg.5788; -.
DR eggNOG; COG0535; Bacteria.
DR HOGENOM; CLU_009273_4_7_6; -.
DR OMA; IVWNFTN; -.
DR OrthoDB; 1172757at2; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009975; F:cyclase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00660; PqqE; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR011843; PQQ_synth_PqqE_bac.
DR InterPro; IPR017200; PqqE-like.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR PIRSF; PIRSF037420; PQQ_syn_pqqE; 1.
DR SFLD; SFLDF00280; coenzyme_PQQ_synthesis_protein; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR02109; PQQ_syn_pqqE; 1.
DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; PQQ biosynthesis;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..389
FT /note="PqqA peptide cyclase"
FT /id="PRO_0000219944"
FT DOMAIN 20..235
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 34
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00660"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00660"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00660"
SQ SEQUENCE 389 AA; 43753 MW; E3E9912DF6E5D26A CRC64;
MLSTGSNSPE AAVLPGKPEV GLPLWLLAEL TYRCPLQCPY CSNPLDFAEQ GKELSTEQWI
KVFREAREMG AAQLGFSGGE PLVRQDLAEL IGEARKLGFY TNLITSGIGL TEQKISDFKK
AGLDHIQISF QASDEQVNNL LAGSKKAFAQ KLEMARAVKA HGYPMVLNFV THRHNIDKID
RIIELCIALE ADFVELATCQ FYGWAQLNRV GLLPTKEQLV RAERITNEYR ARLEAQGHLC
KLIFVTPDYY EERPKACMNG WGSIFLTVTP DGTALPCHGA RQMPVQFPNV RDHSMQHIWY
DSFGFNRFRG YDWMPEPCRS CDEKEKDFGG CRCQAFMLTG DASNADPVCS KSPHHGMILQ
AREESETATH TIEQLAFRNE RNSRLIAKG
