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7-carboxy-7-deazaguanine synthase (CDG synthase) (EC 4.3.99.3) (Queuosine biosynthesis protein QueE)

 K0Z3D9_9STRE            Unreviewed;       238 AA.
K0Z3D9;
28-NOV-2012, integrated into UniProtKB/TrEMBL.
28-NOV-2012, sequence version 1.
25-OCT-2017, entry version 30.
RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000256|HAMAP-Rule:MF_00917};
Short=CDG synthase {ECO:0000256|HAMAP-Rule:MF_00917};
EC=4.3.99.3 {ECO:0000256|HAMAP-Rule:MF_00917};
AltName: Full=Queuosine biosynthesis protein QueE {ECO:0000256|HAMAP-Rule:MF_00917};
Name=queE {ECO:0000256|HAMAP-Rule:MF_00917};
ORFNames=GMD4S_12357 {ECO:0000313|EMBL:EKA01775.1};
Streptococcus sp. GMD4S.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=1169673 {ECO:0000313|EMBL:EKA01775.1, ECO:0000313|Proteomes:UP000004724};
[1] {ECO:0000313|EMBL:EKA01775.1, ECO:0000313|Proteomes:UP000004724}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GMD4S {ECO:0000313|EMBL:EKA01775.1,
ECO:0000313|Proteomes:UP000004724};
PubMed=23493677; DOI=10.1101/gr.142208.112;
Fitzsimons M.S., Novotny M., Lo C.C., Dichosa A.E.,
Yee-Greenbaum J.L., Snook J.P., Gu W., Chertkov O., Davenport K.W.,
McMurry K., Reitenga K.G., Daughton A.R., He J., Johnson S.L.,
Gleasner C.D., Wills P.L., Parson-Quintana B., Chain P.S.,
Detter J.C., Lasken R.S., Han C.S.;
"Nearly finished genomes produced using gel microdroplet culturing
reveal substantial intraspecies genomic diversity within the human
microbiome.";
Genome Res. 23:878-888(2013).
-!- FUNCTION: Catalyzes the complex heterocyclic radical-mediated
conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-
carboxy-7-deazaguanine (CDG), a step common to the biosynthetic
pathways of all 7-deazapurine-containing compounds.
{ECO:0000256|HAMAP-Rule:MF_00917}.
-!- CATALYTIC ACTIVITY: 6-carboxy-5,6,7,8-tetrahydropterin = 7-
carboxy-7-carbaguanine + NH(3). {ECO:0000256|HAMAP-Rule:MF_00917}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
-!- COFACTOR:
Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
Note=Binds 1 S-adenosyl-L-methionine per subunit.
{ECO:0000256|HAMAP-Rule:MF_00917};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
cysteines and an exchangeable S-adenosyl-L-methionine.
{ECO:0000256|HAMAP-Rule:MF_00917};
-!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00917}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00917}.
-!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7-
deazaguanine synthase family. {ECO:0000256|HAMAP-Rule:MF_00917}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00917}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EKA01775.1}.
-----------------------------------------------------------------------
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EMBL; AJRE01000494; EKA01775.1; -; Genomic_DNA.
RefSeq; WP_000196454.1; NZ_AJRE01000494.1.
ProteinModelPortal; K0Z3D9; -.
EnsemblBacteria; EKA01775; EKA01775; GMD4S_12357.
PATRIC; fig|1169673.3.peg.2059; -.
UniPathway; UPA00391; -.
Proteomes; UP000004724; Unassembled WGS sequence.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 3.80.30.20; -; 1.
HAMAP; MF_00917; QueE; 1.
InterPro; IPR024924; 7-CO-7-deazaguanine_synth-like.
InterPro; IPR017742; Deazaguanine_synth.
InterPro; IPR007197; rSAM.
InterPro; IPR023404; rSAM_horseshoe.
Pfam; PF04055; Radical_SAM; 1.
PIRSF; PIRSF000370; QueE; 1.
SFLD; SFLDF00300; 7-carboxy-7-deazaguanine_synth; 1.
SFLD; SFLDS00029; Radical_SAM; 1.
TIGRFAMs; TIGR03365; Bsubt_queE; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00917};
Complete proteome {ECO:0000313|Proteomes:UP000004724};
Iron {ECO:0000256|HAMAP-Rule:MF_00917};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00917};
Lyase {ECO:0000256|HAMAP-Rule:MF_00917};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00917};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00917};
Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00917};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00917}.
DOMAIN 33 126 Radical_SAM. {ECO:0000259|Pfam:PF04055}.
REGION 19 21 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00917}.
REGION 44 46 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_00917}.
REGION 128 130 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 38 38 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 42 42 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 45 45 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 47 47 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00917}.
BINDING 34 34 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00917}.
BINDING 81 81 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00917}.
BINDING 83 83 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00917}.
SEQUENCE 238 AA; 26722 MW; 042C4D01647AD7EF CRC64;
MTRERVLKLP VLEIFGPTFQ GEGRAIGQKT MFVRTAGCDY HCDWCDSAFT WDGSEKPTRM
TADEVIAALD KLGNYDYVTL SGGNPAILAA NMAQLVTKLK ERGVTLAVET QGSRWQNWLK
DIDQVTLSPK PPSSKMEVNF ETLDFIVSQL DPDKVTFKIP VFDDADLAFA RGIQERYQPD
VLFLSAGNPE PKATGNIVQD QLDRLKELWE RIAADDSWGN VRVLPQLHTL LYDNQRGV


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