ID   PQQE_RAHAQ              Reviewed;         377 AA.
AC   O33506;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=PqqA peptide cyclase;
DE            EC=1.21.98.4;
DE   AltName: Full=Coenzyme PQQ synthesis protein E;
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein E;
GN   Name=pqqE;
OS   Rahnella aquatilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Rahnella.
OX   NCBI_TaxID=34038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ISL19;
RX   PubMed=9485602; DOI=10.1111/j.1574-6968.1998.tb12850.x;
RA   Kim K.Y., Jordan D., Krishnan H.B.;
RT   "Expression of genes from Rahnella aquatilis that are necessary for mineral
RT   phosphate solubilization in Escherichia coli.";
RL   FEMS Microbiol. Lett. 159:121-127(1998).
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).
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;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC   -!- SUBUNIT: Interacts with PqqD. The interaction is necessary for activity
CC       of PqqE.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. PqqE family.
CC       {ECO:0000305}.
CC   -!- CAUTION: An expected iron ligand Cys residue was not found at position
CC       29 in this sequence. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC38153.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF007584; AAC38153.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; O33506; -.
DR   SMR; O33506; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR02109; PQQ_syn_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..377
FT                   /note="PqqA peptide cyclase"
FT                   /id="PRO_0000219949"
FT   DOMAIN          8..224
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         22
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         26
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   377 AA;  42317 MW;  3439ACEAF9B5A757 CRC64;
     MNLLKPAVKP PSWLLAELTY RCPVQCPYWS NPLDFAKQEK ELTTAQWIKV FEEAREMGAV
     QIGFSGGEPL VRKDLPELIR GARDLGFYTN LITSGIGLTE KKIDAFAQAG LDHIQISFQA
     SDEELNAALA GNAKAFQQKL AMAKAVKAHG YPMVLNFVLH RHNIDQIDKI IDLSIELDAD
     DVELATCQFY GWAQLNREGL LPTREQIARA EDVVHQYREK MAGTGNLANL LFVTPDYYEE
     RPKGCMGGWG AIFLSVTPEG MALPCHSARQ LPVEFPSVLE NTLQEIWYDS FGFNKYRGFD
     WMPEPCRSCS EKEKDFGGCR CQAFMLTGNA DNADPVCSKS EHHGMILAAR EQANCTNIQI
     NQLQFRNRAN SQLIFKG