ID A0A257R3Z5_9PROT Unreviewed; 371 AA.
AC A0A257R3Z5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=PqqA peptide cyclase {ECO:0000256|HAMAP-Rule:MF_00660};
DE EC=1.21.98.4 {ECO:0000256|HAMAP-Rule:MF_00660};
DE AltName: Full=Coenzyme PQQ synthesis protein E {ECO:0000256|HAMAP-Rule:MF_00660};
GN Name=pqqE {ECO:0000256|HAMAP-Rule:MF_00660};
GN ORFNames=B7Z76_09195 {ECO:0000313|EMBL:OYV55723.1};
OS Acidiphilium sp. 20-67-58.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=1970291 {ECO:0000313|EMBL:OYV55723.1, ECO:0000313|Proteomes:UP000216756};
RN [1] {ECO:0000313|EMBL:OYV55723.1, ECO:0000313|Proteomes:UP000216756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20-67-58 {ECO:0000313|EMBL:OYV55723.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:0000256|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:0000256|HAMAP-Rule:MF_00660};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00660};
CC -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00660}.
CC -!- SUBUNIT: Interacts with PqqD. The interaction is necessary for activity
CC of PqqE. {ECO:0000256|HAMAP-Rule:MF_00660}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. PqqE family.
CC {ECO:0000256|HAMAP-Rule:MF_00660}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYV55723.1}.
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DR EMBL; NCAS01000019; OYV55723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257R3Z5; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000216756; Unassembled WGS sequence.
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; IPR034391; Cmo-like_SPASM_containing.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
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; SFLDG01387; BtrN-like_SPASM_domain_contain; 1.
DR SFLD; SFLDF00280; coenzyme_PQQ_synthesis_protein; 1.
DR SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00660};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00660};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00660};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00660};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00660};
KW PQQ biosynthesis {ECO:0000256|ARBA:ARBA00022905, ECO:0000256|HAMAP-
KW Rule:MF_00660};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00660}.
FT DOMAIN 14..231
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 28
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00660"
FT BINDING 32
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00660"
FT BINDING 35
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00660"
SQ SEQUENCE 371 AA; 40505 MW; EB08B056C3448CDC CRC64;
MNDLAPASVT RAAVAPPMAI MMELTHRCPL KCPYCSNPLA MDRARDEMDT ATWMRVITEA
AALGALQGHF SGGEPMARDD LAQLVQHAHR EGLYTNLITS AVLLDQQKMH MLAEAGLDHV
QISFQGAESG IADHVAGLRN AHVKKLAAAR LVRDAGLALT VNAVMHRQNL HQLPAMLDLA
VEAGAQRIEV AHVQYYGWAL KNRAALIPTR GQLDEATRIV DEARKRLEGV LNIDYVVPDY
YASRPKSCMS GWARRFFNVT PSGKVLPCHA AETIGHLRFD SVKDKSLAEI WLNSEAFNAY
RGTDWMPAPC KGCERAEIDW GGCRCQALAI AGDAGATDPA CSLSPHHDRM LNLAVEESAA
GSEAFVYRMI S
//
