ID L0A1U6_DEIPD Unreviewed; 230 AA.
AC L0A1U6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000256|HAMAP-Rule:MF_00917};
DE Short=CDG synthase {ECO:0000256|HAMAP-Rule:MF_00917};
DE EC=4.3.99.3 {ECO:0000256|HAMAP-Rule:MF_00917};
DE AltName: Full=Queuosine biosynthesis protein QueE {ECO:0000256|HAMAP-Rule:MF_00917};
GN Name=queE {ECO:0000256|HAMAP-Rule:MF_00917};
GN OrderedLocusNames=Deipe_2338 {ECO:0000313|EMBL:AFZ67816.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ67816.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00917};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
CC Note=Binds 1 S-adenosyl-L-methionine per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00917};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00917};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00917}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00917}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7-
CC deazaguanine synthase family. {ECO:0000256|HAMAP-Rule:MF_00917}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00917}.
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DR EMBL; CP003382; AFZ67816.1; -; Genomic_DNA.
DR RefSeq; WP_015236118.1; NC_019793.1.
DR AlphaFoldDB; L0A1U6; -.
DR STRING; 937777.Deipe_2338; -.
DR KEGG; dpd:Deipe_2338; -.
DR PATRIC; fig|937777.3.peg.2339; -.
DR eggNOG; COG0602; Bacteria.
DR HOGENOM; CLU_066739_0_1_0; -.
DR OrthoDB; 9792276at2; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000010467; 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 GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 PANTHER; PTHR42836; 7-CARBOXY-7-DEAZAGUANINE SYNTHASE; 1.
DR PANTHER; PTHR42836:SF1; 7-CARBOXY-7-DEAZAGUANINE SYNTHASE; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000370; QueE; 1.
DR SFLD; SFLDS00029; Radical_SAM; 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_00917};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00917};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00917};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00917};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00917};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00917}; Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00917};
KW Reference proteome {ECO:0000313|Proteomes:UP000010467};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00917}.
FT DOMAIN 18..209
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 12..14
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 31
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_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:0000256|HAMAP-Rule:MF_00917"
FT BINDING 37..39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 38
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_00917"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 121..123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
SQ SEQUENCE 230 AA; 25640 MW; 256AAE08477F8E9A CRC64;
MKYPVHERFY TWQGEGVHLG RAAYFVRLYG CPQACPWCDS AGTWHTEFRP ERVSLMTPRE
IAAGVERESP SGAVVVVTGG EPILFDLAPL VGELHALGRA VHLETSGIAE LRGEIDWVTL
SPKPFGTWPL PSVVARTDEV KIIVHDVLDI DAGLRTLSGL RDDAVIWLHP EWSKARDRDR
RVLNAITEAV KQNPRLRAGY QMHKLYRADD LDANSVKTLI PLGGNPELGY
//
