PQQE_METEP
ID PQQE_METEP Reviewed; 384 AA.
AC A9W3R0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Mext_1817;
OS Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=419610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Marx C., Richardson P.;
RT "Complete sequence of Methylobacterium extorquens PA1.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000908; ABY30216.1; -; Genomic_DNA.
DR RefSeq; WP_012253377.1; NC_010172.1.
DR AlphaFoldDB; A9W3R0; -.
DR SMR; A9W3R0; -.
DR STRING; 419610.Mext_1817; -.
DR EnsemblBacteria; ABY30216; ABY30216; Mext_1817.
DR KEGG; mex:Mext_1817; -.
DR eggNOG; COG0535; Bacteria.
DR HOGENOM; CLU_009273_4_7_5; -.
DR OMA; GWGRQFF; -.
DR BioCyc; MEXT419610:MEXT_RS09205-MON; -.
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; 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 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 S-adenosyl-L-methionine.
FT CHAIN 1..384
FT /note="PqqA peptide cyclase"
FT /id="PRO_1000131277"
FT DOMAIN 14..230
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 28
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 32
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 35
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 384 AA; 41677 MW; 49B7727E353A1559 CRC64;
MNAPTPAPSP VDVIPAPVGL LAELTHRCPL RCPYCSNPLE LDRRSAELDT QTWLRVLTEA
AGLGVLHVHL SGGEPTARPD IVEITAKCAE LGLYSNLITS GVGGALAKLD ALYDVGLDHV
QLSVQGVDAA NAEKIGGLKN AQPQKMQFAA RVTELGLPLT LNSVIHRGNI HEVPGFIDLA
VKLGAKRLEV AHTQYYGWAY VNRAALMPDK SQVDESIRIV EAARERLKGQ LVIDLVVPDY
YAKYPKACAG GWGRKLMNVT PQGKVLPCHA AETIPGLEFW YVTDHSLGEI WTQSPAFAAY
RGTSWMKEPC RSCDRREKDW GGCRCQALAL TGDAANTDPA CSLSPLHAKM RDLAKEEAAE
TPPDYIYRSI GTNVQNPLSE KAPL
