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PQQE_METPB
ID   PQQE_METPB              Reviewed;         384 AA.
AC   B1ZIB2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Mpop_1769;
OS   Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS   (Methylobacterium populi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=441620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL   Submitted (APR-2008) 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; CP001029; ACB79932.1; -; Genomic_DNA.
DR   RefSeq; WP_012453678.1; NC_010725.1.
DR   AlphaFoldDB; B1ZIB2; -.
DR   SMR; B1ZIB2; -.
DR   STRING; 441620.Mpop_1769; -.
DR   EnsemblBacteria; ACB79932; ACB79932; Mpop_1769.
DR   KEGG; mpo:Mpop_1769; -.
DR   eggNOG; COG0535; Bacteria.
DR   HOGENOM; CLU_009273_4_7_5; -.
DR   OMA; GWGRQFF; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000007136; 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; 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   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..384
FT                   /note="PqqA peptide cyclase"
FT                   /id="PRO_1000131278"
FT   DOMAIN          14..226
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;  41528 MW;  EED7D614A788B61D CRC64;
     MNAPTPAPSP ADVIPAPVGL LAELTHRCPL RCPYCSNPLE LDRRSAELDT QAWLRVLTEA
     AGLGVLHVHL SGGEPTARPD IVEITAKCAE LGLYSNLITS GVGGALAKLD ALYDAGLDHV
     QLSVQGVDAA NAEKIGGLKN AQPQKMQFAA RVTELGLPLT LNSVIHRGNI HEVPGFIDLA
     VKLGAKRLEV AHTQYYGWAY VNRAALMPDK AQVDESIRIV EAARERLKGQ LVIDLVVPDY
     YAKYPKACAG GWGRKLMNVT PQGKVLPCHA AETIPGLEFW YVTDHALGDI WTKSPAFAAY
     RGTGWMKEPC RSCDRREKDW GGCRCQALAL TGDAANTDPA CSLSPLHAKM RDLAKEEAAE
     NPPDYIYRSI GTNVQNPLSE KAPL
 
 
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