ID PQQE_GLUOX Reviewed; 358 AA.
AC Q9L3B0; Q5FS91;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 27-MAR-2024, entry version 121.
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=GOX0983;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9937 / LMG 1404 / NCIMB 8084;
RX PubMed=11111029; DOI=10.1111/j.1574-6968.2000.tb09429.x;
RA Felder M., Gupta A., Verma V., Kumar A., Qazi G.N., Cullum J.;
RT "The pyrroloquinoline quinone synthesis genes of Gluconobacter oxydans.";
RL FEMS Microbiol. Lett. 193:231-236(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; AJ277117; CAB83201.1; -; Genomic_DNA.
DR EMBL; CP000009; AAW60755.1; -; Genomic_DNA.
DR RefSeq; WP_011252550.1; NZ_LT900338.1.
DR AlphaFoldDB; Q9L3B0; -.
DR SMR; Q9L3B0; -.
DR STRING; 290633.GOX0983; -.
DR KEGG; gox:GOX0983; -.
DR eggNOG; COG0535; Bacteria.
DR HOGENOM; CLU_009273_4_7_5; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000006375; 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 CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21119; SPASM_PqqE; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00660; PqqE; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
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 NCBIfam; TIGR02109; PQQ_syn_pqqE; 1.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR PANTHER; PTHR11228:SF7; PQQA PEPTIDE CYCLASE; 1.
DR PANTHER; PTHR11228; RADICAL SAM DOMAIN PROTEIN; 1.
DR Pfam; PF13353; Fer4_12; 1.
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 SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 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..358
FT /note="PqqA peptide cyclase"
FT /id="PRO_0000219939"
FT DOMAIN 4..219
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 18
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 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 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 CONFLICT 120
FT /note="A -> G (in Ref. 1; CAB83201)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="V -> I (in Ref. 1; CAB83201)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="E -> D (in Ref. 1; CAB83201)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="V -> I (in Ref. 1; CAB83201)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="A -> S (in Ref. 1; CAB83201)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="Q -> K (in Ref. 1; CAB83201)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="M -> L (in Ref. 1; CAB83201)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="V -> I (in Ref. 1; CAB83201)"
FT /evidence="ECO:0000305"
FT CONFLICT 334..358
FT /note="YHDRVEQAVENNMQPESTLFYRRYT -> FTILWNRQGVKKQNLSIGGGKVR
FT SVF (in Ref. 1; CAB83201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 39656 MW; 1E9697C12C8DD949 CRC64;
MTLPSPPMSL LAELTHRCPL SCPYCSNPLE LERKAAELDT ATWTAVLEQA AELGVLQVHF
SGGEPMARPD LVELVSVARR LNLYSNLITS GVLLDEPKLE ALDRAGLDHI QLSFQDVTEA
GAERIGGLKG AQARKVAAAR LIRASGIPMT LNFVVHRENV ARIPEMFALA RELGAGRVEI
AHTQYYGWGL KNREALLPSR DQLEESTRAV EAERAKGGLS VDYVTPDYHA DRPKPCMGGW
GQRFVNVTPS GRVLPCHAAE IIPDVAFPNV QDVTLSEIWN ISPLFNMFRG TDWMPEPCRS
CERKERDWGG CRCQAMALTG NAANTDPVCS LSPYHDRVEQ AVENNMQPES TLFYRRYT
//
