QUEE_PYRAE
ID QUEE_PYRAE Reviewed; 222 AA.
AC Q8ZZZ0;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_00917};
DE Short=CDG synthase {ECO:0000255|HAMAP-Rule:MF_00917};
DE EC=4.3.99.3 {ECO:0000255|HAMAP-Rule:MF_00917};
DE AltName: Full=Archaeosine biosynthesis protein QueE {ECO:0000255|HAMAP-Rule:MF_00917};
GN Name=queE {ECO:0000255|HAMAP-Rule:MF_00917}; OrderedLocusNames=PAE0010;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC -!- FUNCTION: Catalyzes the complex heterocyclic radical-mediated
CC conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-
CC deazaguanine (CDG), a step common to the biosynthetic pathways of all
CC 7-deazapurine-containing compounds. {ECO:0000255|HAMAP-Rule:MF_00917}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-
CC deazaguanine + NH4(+); Xref=Rhea:RHEA:27974, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:61032, ChEBI:CHEBI:61036; EC=4.3.99.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917};
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_00917};
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917};
CC Note=Binds 1 S-adenosyl-L-methionine per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00917};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00917}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00917}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7-
CC deazaguanine synthase family. {ECO:0000255|HAMAP-Rule:MF_00917}.
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DR EMBL; AE009441; AAL62499.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZZZ0; -.
DR SMR; Q8ZZZ0; -.
DR STRING; 178306.PAE0010; -.
DR EnsemblBacteria; AAL62499; AAL62499; PAE0010.
DR KEGG; pai:PAE0010; -.
DR PATRIC; fig|178306.9.peg.8; -.
DR eggNOG; arCOG02173; Archaea.
DR HOGENOM; CLU_066739_2_4_2; -.
DR InParanoid; Q8ZZZ0; -.
DR OMA; CKGFNCK; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00917; QueE; 1.
DR InterPro; IPR024924; 7-CO-7-deazaguanine_synth-like.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000370; QueE; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Magnesium; Metal-binding;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..222
FT /note="7-carboxy-7-deazaguanine synthase"
FT /id="PRO_0000416221"
FT DOMAIN 22..222
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 16..18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 35
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_00917"
FT BINDING 39
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_00917"
FT BINDING 42
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_00917"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 126..128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
SQ SEQUENCE 222 AA; 24359 MW; 22A0EA977CDB0316 CRC64;
MSATPRVRVL EIFASLQGEG INLGRPAVFV RLAGCPIRCI YCDTKYSWDF NAGVEMGVEE
IVAKALALSV VGHVVVTGGE PLIWQRRGLE ELACALRALG SVEVETSGAY PPTPELDRCV
DFYDVSPKLS NAGVKAPFSP FYASSPKAWF KFVVSNADDV EEVERFVVAY GIPRGRVFLM
PMAESPEEHG EALRRIWDAA VRGGFRVTPR LHIMAWGNAR GK
