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

 M5R5F7_9BACI            Unreviewed;       240 AA.
M5R5F7;
29-MAY-2013, integrated into UniProtKB/TrEMBL.
29-MAY-2013, sequence version 1.
25-OCT-2017, entry version 27.
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=F510_2720 {ECO:0000313|EMBL:EMI09209.1};
Anoxybacillus sp. DT3-1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
NCBI_TaxID=690871 {ECO:0000313|EMBL:EMI09209.1, ECO:0000313|Proteomes:UP000011915};
[1] {ECO:0000313|EMBL:EMI09209.1, ECO:0000313|Proteomes:UP000011915}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DT3-1 {ECO:0000313|EMBL:EMI09209.1,
ECO:0000313|Proteomes:UP000011915};
PubMed=24603481;
Goh K.M., Gan H.M., Chan K.G., Chan G.F., Shahar S., Chong C.S.,
Kahar U.M., Chai K.P.;
"Analysis of anoxybacillus genomes from the aspects of lifestyle
adaptations, prophage diversity, and carbohydrate metabolism.";
PLoS ONE 9:E90549-E90549(2014).
-!- 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:EMI09209.1}.
-----------------------------------------------------------------------
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EMBL; ANMT01000034; EMI09209.1; -; Genomic_DNA.
RefSeq; WP_009362721.1; NZ_ANMT01000034.1.
ProteinModelPortal; M5R5F7; -.
EnsemblBacteria; EMI09209; EMI09209; F510_2720.
PATRIC; fig|690871.3.peg.2705; -.
UniPathway; UPA00391; -.
Proteomes; UP000011915; 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:UP000011915};
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 28 123 Radical_SAM. {ECO:0000259|Pfam:PF04055}.
REGION 14 16 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00917}.
REGION 39 41 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_00917}.
REGION 126 128 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 33 33 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 37 37 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 40 40 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 42 42 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00917}.
BINDING 29 29 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00917}.
BINDING 80 80 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00917}.
BINDING 82 82 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00917}.
SEQUENCE 240 AA; 27697 MW; 99BD8A13393C58D7 CRC64;
MERIPVIEIF GPTIQGEGMV IGQKTMFVRT AGCDYRCRWC DSSFTWDGSA KDEIKQMTPE
HIWQQLKQLG GDRFNHVTIS GGNPALLKSL HALISLLKQH RMRIGLETQG SVWQDWFYDI
DDLTISPKPP SSNMETNFAM LDTIMDRLAM HRGQVSLKVV VFNDEDFAYA KHVHQRYPTV
PFYVQVGNDD IHEADDMTLR LKLLQKLEWL VEQVVQSNEM NDVRVLPQLH TLLWGNRRGV


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