PQQE_METEA
ID PQQE_METEA Reviewed; 384 AA.
AC P71517; C5B128;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=PqqA peptide cyclase {ECO:0000305};
DE EC=1.21.98.4 {ECO:0000269|PubMed:25817994, ECO:0000269|PubMed:26961875};
DE AltName: Full=Coenzyme PQQ synthesis protein E {ECO:0000305};
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein E;
GN Name=pqqE; OrderedLocusNames=MexAM1_META1p1748;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9043136; DOI=10.1099/00221287-143-2-595;
RA Toyama H., Chistoserdova L., Lidstrom M.E.;
RT "Sequence analysis of pqq genes required for biosynthesis of
RT pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the
RT purification of a biosynthetic intermediate.";
RL Microbiology 143:595-602(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH PQQD.
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=25817994; DOI=10.1074/jbc.m115.646521;
RA Latham J.A., Iavarone A.T., Barr I., Juthani P.V., Klinman J.P.;
RT "PqqD is a novel peptide chaperone that forms a ternary complex with the
RT radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone
RT biosynthetic pathway.";
RL J. Biol. Chem. 290:12908-12918(2015).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=26961875; DOI=10.1074/jbc.c115.699918;
RA Barr I., Latham J.A., Iavarone A.T., Chantarojsiri T., Hwang J.D.,
RA Klinman J.P.;
RT "Demonstration that the radical S-adenosylmethionine (SAM) enzyme PqqE
RT catalyzes de novo carbon-carbon cross-linking within a peptide substrate
RT PqqA in the presence of the peptide chaperone PqqD.";
RL J. Biol. Chem. 291:8877-8884(2016).
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:0000269|PubMed:25817994}.
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:0000269|PubMed:25817994};
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:25817994}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. PqqE family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACS39592.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U72662; AAB58898.1; -; Genomic_DNA.
DR EMBL; CP001510; ACS39592.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003597604.1; NC_012808.1.
DR PDB; 6C8V; X-ray; 3.20 A; A=12-384.
DR PDBsum; 6C8V; -.
DR AlphaFoldDB; P71517; -.
DR SMR; P71517; -.
DR STRING; 272630.MexAM1_META1p1748; -.
DR EnsemblBacteria; ACS39592; ACS39592; MexAM1_META1p1748.
DR KEGG; mea:Mex_1p1748; -.
DR eggNOG; COG0535; Bacteria.
DR HOGENOM; CLU_009273_4_7_5; -.
DR OrthoDB; 1172757at2; -.
DR BRENDA; 1.21.98.4; 3296.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000009081; 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; 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 SFLD; SFLDS00029; Radical_SAM; 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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW PQQ biosynthesis; S-adenosyl-L-methionine.
FT CHAIN 1..384
FT /note="PqqA peptide cyclase"
FT /id="PRO_0000219941"
FT DOMAIN 14..230
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 28
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT CONFLICT 293..296
FT /note="KSPA -> SHGR (in Ref. 1; AAB58898)"
FT /evidence="ECO:0000305"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:6C8V"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:6C8V"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6C8V"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:6C8V"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:6C8V"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:6C8V"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:6C8V"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 210..226
FT /evidence="ECO:0007829|PDB:6C8V"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:6C8V"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:6C8V"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:6C8V"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6C8V"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:6C8V"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:6C8V"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:6C8V"
SQ SEQUENCE 384 AA; 41661 MW; CC668B9BF6C62A9A CRC64;
MNAPTPAPSP VDVIPAPVGL LAELTHRCPL RCPYCSNPLE LDRRSAELDT QTWLRVLTEA
AGLGVLHVHL SGGEPTARPD IVEITAKCAE LGLYSNLITS GVGGALAKLD ALYDVGLDHV
QLSVQGVDAA NAEKIGGLKN AQPQKMQFAA RVTELGLPLT LNSVIHRGNI HEVPGFIDLA
VKLGAKRLEV AHTQYYGWAY VNRAALMPDK SQVDESIRIV EAARERLKGQ LVIDLVVPDY
YAKYPKACAG GWGRKLMNVT PQGKVLPCHA AETIPGLEFW YVTDHALGEI WTKSPAFAAY
RGTSWMKEPC RSCDRREKDW GGCRCQALAL TGDAANTDPA CSLSPLHAKM RDLAKEEAAE
TPPDYIYRSI GTNVQNPLSE KAPL
