PQQE_ACICA
ID PQQE_ACICA Reviewed; 384 AA.
AC P07782; Q43987; Q9JN48;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=PqqA peptide cyclase;
DE EC=1.21.98.4;
DE AltName: Full=Coenzyme PQQ synthesis protein E;
DE AltName: Full=Coenzyme PQQ synthesis protein III;
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein E;
GN Name=pqqE; Synonyms=pqqIII;
OS Acinetobacter calcoaceticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=471;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LMD 79.41;
RX PubMed=2536663; DOI=10.1128/jb.171.1.447-455.1989;
RA Goosen N., Horsman H.P.A., Huinen R.G.M., van de Putte P.;
RT "Acinetobacter calcoaceticus genes involved in biosynthesis of the coenzyme
RT pyrrolo-quinoline-quinone: nucleotide sequence and expression in
RT Escherichia coli K-12.";
RL J. Bacteriol. 171:447-455(1989).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAB89080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X06452; CAA29756.1; -; Genomic_DNA.
DR EMBL; X06452; CAB89080.1; ALT_INIT; Genomic_DNA.
DR PIR; F32252; F32252.
DR AlphaFoldDB; P07782; -.
DR SMR; P07782; -.
DR STRING; 471.BUM88_09600; -.
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 TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 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..384
FT /note="PqqA peptide cyclase"
FT /id="PRO_0000219934"
FT DOMAIN 5..220
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 23
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 384 AA; 43665 MW; 9CB2EAE80CD3ECAF CRC64;
MTEGVGLPLW LLAELTYRCP LQCPYCSNPL DYAQHKNELT TQEWFDVFDQ ARQMGAVQLG
FSGGEPLVRQ DLEQLVAHAH QQGFYTNLIT SGMGLTEQRI ADLKQAGLDH IQVSFQASDP
VVNDALAGSK HAFEQKYEMC RLVKKYDYPM VLNFVIHRHN IDQIEQIIEL CLELNADTVE
LAICQFYGWA FLNRQGLLPT QEQLTRAERI TNEYREKLKA QNHPCKLIFV VPDYYEERPK
ACMNGWGKIF FTVAPDGMAL PCHAARQLPI SFPNVREHKL SDIWYKSTGF NHFRGDAWMP
EGCRSCPDKD RDFGGCRCQA YMLTGDAANA DPVCGKSPYH QMIEQARAES QLVAPLQNLV
FRNSRNSKSL SATQNIPVHT ITDI
