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Database: UniProt
Entry: D9WCB4_9ACTN
LinkDB: D9WCB4_9ACTN
Original site: D9WCB4_9ACTN 
ID   D9WCB4_9ACTN            Unreviewed;       371 AA.
AC   D9WCB4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 74.
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=SSOG_00573 {ECO:0000313|EMBL:EFL20861.1};
OS   Streptomyces himastatinicus ATCC 53653.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL20861.1, ECO:0000313|Proteomes:UP000003963};
RN   [1] {ECO:0000313|EMBL:EFL20861.1, ECO:0000313|Proteomes:UP000003963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL20861.1,
RC   ECO:0000313|Proteomes:UP000003963};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL   Submitted (FEB-2009) 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}.
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DR   EMBL; GG657754; EFL20861.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9WCB4; -.
DR   STRING; 457427.SSOG_00573; -.
DR   HOGENOM; CLU_009273_4_7_11; -.
DR   OrthoDB; 9782387at2; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000003963; 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; 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; ANTILISTERIAL BACTERIOCIN SUBTILOSIN BIOSYNTHESIS PROTEIN ALBA; 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; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, 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          11..226
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          350..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         25
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         29
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"
SQ   SEQUENCE   371 AA;  39966 MW;  4B711B448CD56A1A CRC64;
     MDTVTAHPQG HPRPWALLAE LTHGCPLHCP YCSNPLQLTR RSRELTGEEW ERVLRQAAEL
     GVVHTHLSGG EPLLRRDLEV IVAAAASAGL YTQLVTSGVG LDEARLTALT GAGLHSVQLS
     VQHADPGASD RIAGHRSFAA KERAAALVRE AGLPLGVNVV LHRDNLDALD PLIELAVAWG
     ADRVELANTQ FYGWALRNRA ALLPTREQLA RAREGVARWR EKLGGRTELV WVLPDYFEGV
     AKPCMGGWGA VSLTVAPDGT VLPCPAAAAL PGLDPPNVRD HALEWIWDHS AAFNRYRGEE
     WMAEPCRSCS HRAEDFGGCR CQAYALTGDA ARTDPACALS PDHGLIRSLT GPAPAAEPPP
     PGYTYRGYGR G
//
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