ID   PQQE_KLEP7              Reviewed;         380 AA.
AC   A6T9H2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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};
GN   OrderedLocusNames=KPN78578_17820; ORFNames=KPN_01812;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000647; ABR77243.1; -; Genomic_DNA.
DR   RefSeq; WP_015958461.1; NC_009648.1.
DR   AlphaFoldDB; A6T9H2; -.
DR   SMR; A6T9H2; -.
DR   STRING; 272620.KPN_01812; -.
DR   EnsemblBacteria; ABR77243; ABR77243; KPN_01812.
DR   KEGG; kpn:KPN_01812; -.
DR   HOGENOM; CLU_009273_4_7_6; -.
DR   OMA; GWGRQFF; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000000265; 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; 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   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   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..380
FT                   /note="PqqA peptide cyclase"
FT                   /id="PRO_1000061915"
FT   DOMAIN          8..223
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:0000255|HAMAP-Rule:MF_00660"
FT   BINDING         26
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         29
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   380 AA;  42971 MW;  BFBA75F653129F3B CRC64;
     MNQSKPTVNP PLWLLAELTY RCPLQCPYCS NPLDFARQDK ELTTEQWIEV FRQARAMGSV
     QLGFSGGEPL TRKDLPELIR AARDLGFYTN LITSGIGLTE SKLDAFSEAG LDHIQISFQA
     SDEVLNAALA GNKKAFQQKL TMAKAVKARD YPMVLNFVLH RHNIDQLDKI IELCIELEAD
     DVELATCQFY GWAFLNREGL LPTREQIARA EQVVADYRQK MAASGNLTNL LFVTPDYYEE
     RPKGCMGGWG SIFLSVTPEG TALPCHSARQ LPVAFPSVLE QSLESIWYDS FGFNRYRGYD
     WMPEPCRSCD EKEKDFGGCR CQAFMLTGSA DNADPVCSKS PHHHKILEAR REAACSDIKV
     SQLQFRNRTR SQLIYQTRDL