PQQE_KLEPN
ID PQQE_KLEPN Reviewed; 380 AA.
AC P27507;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418;
RX PubMed=1313537; DOI=10.1007/bf00280008;
RA Meulenberg J.J.M., Sellink E., Riegman N.H., Postma P.W.;
RT "Nucleotide sequence and structure of the Klebsiella pneumoniae pqq
RT operon.";
RL Mol. Gen. Genet. 232:284-294(1992).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418;
RX PubMed=7665488; DOI=10.1128/jb.177.17.5088-5098.1995;
RA Velterop J.S., Sellink E., Meulenberg J.J., David S., Bulder I.,
RA Postma P.W.;
RT "Synthesis of pyrroloquinoline quinone in vivo and in vitro and detection
RT of an intermediate in the biosynthetic pathway.";
RL J. Bacteriol. 177:5088-5098(1995).
RN [3]
RP INTERACTION WITH PQQD.
RX PubMed=20737074; DOI=10.1039/c0cc00968g;
RA Wecksler S.R., Stoll S., Iavarone A.T., Imsand E.M., Tran H., Britt R.D.,
RA Klinman J.P.;
RT "Interaction of PqqE and PqqD in the pyrroloquinoline quinone (PQQ)
RT biosynthetic pathway links PqqD to the radical SAM superfamily.";
RL Chem. Commun. (Camb.) 46:7031-7033(2010).
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. {ECO:0000269|PubMed:20737074}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. PqqE family.
CC {ECO:0000305}.
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DR EMBL; X58778; CAA41583.1; -; Genomic_DNA.
DR PIR; S20457; S20457.
DR RefSeq; WP_004184158.1; NZ_WWEY01000125.1.
DR AlphaFoldDB; P27507; -.
DR SMR; P27507; -.
DR BioCyc; MetaCyc:MON-15350; -.
DR BRENDA; 1.21.98.4; 2814.
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; 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 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; PQQ biosynthesis;
KW S-adenosyl-L-methionine.
FT CHAIN 1..380
FT /note="PqqA peptide cyclase"
FT /id="PRO_0000219940"
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: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"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 42914 MW; AAE3EC506FE29816 CRC64;
MSQSKPTVNP PLWLLAELTY RCPLQCPYCS NPLDFARQDK ELTTEQWIEV FRQARAMGSV
QLGFSGGEPL TRKDLPELIR AARDLGFYTN LITSGIGLTE SKLDAFSEAG LDHIQISFQA
SDEVLNAALA GNKKAFQQKL AMAKAVKARD YPMVLNFVLH RHNIDQLDKI IELCIELEAD
DVELATCQFY GWAFLNREGL LPTREQIARA EQVVADYRQK MAASGNLTNL LFVTPDYYEE
RPKGCMGGWG SIFLSVTPEG TALPCHSARQ LPVAFPSVLE QSLESIWYDS FGFNRYRGYD
WMPEPCRSCD EKEKDFGGCR CQAFMLTGSA DNADPVCSKS PHHHKILEAR REAACSDIKV
SQLQFRNRTR SQLIYQTRDL
