ID   PQQE_KLUIN              Reviewed;         374 AA.
AC   P59748;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 71.
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   Kluyvera intermedia (Enterobacter intermedius).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Kluyvera.
OX   NCBI_TaxID=61648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14756528; DOI=10.1007/s00284-003-4068-7;
RA   Kim C.H., Han S.H., Kim K.Y., Cho B.H., Kim Y.H., Koo B.S., Kim Y.C.;
RT   "Cloning and expression of pyrroloquinoline quinone (PQQ) genes from a
RT   phosphate-solubilizing bacterium Enterobacter intermedium.";
RL   Curr. Microbiol. 47:457-461(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; AY216683; AAP34382.1; -; Genomic_DNA.
DR   AlphaFoldDB; P59748; -.
DR   SMR; P59748; -.
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; 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   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   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..374
FT                   /note="PqqA peptide cyclase"
FT                   /id="PRO_0000219938"
FT   DOMAIN          7..222
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         21
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         25
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         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"
SQ   SEQUENCE   374 AA;  41883 MW;  FC5C2430106EBEAF CRC64;
     MNPSKSVTPP LWLLAELTYR CPLQCPYCSN PLDFSQQKKE LTTEQWIEVF RQARAMGSVQ
     LGFSGGEPLT RKDLPELIRA ARDLGFYTNL ITSGIGLTAK KLDAFADAGL DHIQISFQAS
     DETLNAALAG SKKAFQQKLE MAKAVKAHGY PMVLNFVLHR HNIDQIDKII DLCIELDADD
     VELATCQFYG WAQLNREGLL PTREQIANAE AVVADYRQRM GASGNLTNPA VRDAGLLRRA
     AETLHGRMGI DLPQRHADCT ALPCHSARQL PVAFPSVLER TLDDIWYNSF GFNRYRGFDW
     MPEPCRSCDE KAKDFGGCRC QAFMLTGDAD NTDPVCSKSP HHGKILEARR EANCSDIKIQ
     QLQFRNRSNS ELIF