ID   PQQE_STRRO              Reviewed;         364 AA.
AC   P59749; Q83X99;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
OS   Streptomyces rochei (Streptomyces parvullus).
OG   Plasmid pSLA2-L.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces rochei group.
OX   NCBI_TaxID=1928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=7434AN4;
RX   PubMed=12791134; DOI=10.1046/j.1365-2958.2003.03523.x;
RA   Mochizuki S., Hiratsu K., Suwa M., Ishii T., Sugino F., Yamada K.,
RA   Kinashi H.;
RT   "The large linear plasmid pSLA2-L of Streptomyces rochei has an unusually
RT   condensed gene organization for secondary metabolism.";
RL   Mol. Microbiol. 48:1501-1510(2003).
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; AB088224; BAC76463.1; -; Genomic_DNA.
DR   RefSeq; NP_851427.1; NC_004808.2.
DR   RefSeq; WP_011113086.1; NC_004808.2.
DR   AlphaFoldDB; P59749; -.
DR   SMR; P59749; -.
DR   UniPathway; UPA00539; -.
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; 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   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR02109; PQQ_syn_pqqE; 1.
DR   TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Plasmid;
KW   PQQ biosynthesis; S-adenosyl-L-methionine.
FT   CHAIN           1..364
FT                   /note="PqqA peptide cyclase"
FT                   /id="PRO_0000219953"
FT   DOMAIN          6..222
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         20
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         24
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         27
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   364 AA;  38995 MW;  9CDE9A345415A499 CRC64;
     MADPAVGAPA GMLIELTHRC PLHCPYCSNP LELVRREAEL TCEQWTDILT QARELGVVQM
     HFSGGEPLAR PDLPDLVGHA RRLGAYVNLV TSGVGLTAER AHDLARRGVD HVQLSLQDAD
     PAAGQAIAGA RVHTAKLEAA RAVTAAGLPL TVNIVLHRGN IDRTGRMVDL AVDLGADRIE
     LANTQYYGWG LRNRAALMPT AAQLAAAREA VRHARTRYAG GPELVYVAAD YYDDRPKPCM
     DGWGSTQLTV TPAGDVLPCP AAYAITTLPV ENALRRPLSE IWYASRSFNA YRGTGWMREP
     CRTCPERHAD HGGCRCQAFQ LTGDAAATDP ACGLSPHRSL VDAALAEVTD GPVPAFVPRG
     PVPA