QUEE_FLAPJ
ID QUEE_FLAPJ Reviewed; 210 AA.
AC A6H1N2;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Queuosine biosynthesis protein QueE {ECO:0000255|HAMAP-Rule:MF_00917};
GN Name=queE {ECO:0000255|HAMAP-Rule:MF_00917}; OrderedLocusNames=FP2200;
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL44256.1; -; Genomic_DNA.
DR RefSeq; WP_011964290.1; NC_009613.3.
DR RefSeq; YP_001297057.1; NC_009613.3.
DR AlphaFoldDB; A6H1N2; -.
DR SMR; A6H1N2; -.
DR STRING; 402612.FP2200; -.
DR EnsemblBacteria; CAL44256; CAL44256; FP2200.
DR GeneID; 66553304; -.
DR KEGG; fps:FP2200; -.
DR PATRIC; fig|402612.5.peg.2246; -.
DR eggNOG; COG0602; Bacteria.
DR HOGENOM; CLU_066739_0_1_10; -.
DR OMA; CDVKESW; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000006394; 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; -; 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 Queuosine biosynthesis; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..210
FT /note="7-carboxy-7-deazaguanine synthase"
FT /id="PRO_0000416204"
FT DOMAIN 31..210
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 25..27
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 44
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 48
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 51
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 84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 127..129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
SQ SEQUENCE 210 AA; 23981 MW; A73EA0957DB0BB86 CRC64;
MLTKEIQIAV EKGEMLPLME EFYTIQGEGY HTGTAAYFIR IGGCDVGCHW CDVKESWNAA
LHPPTKTDVI VENATKYAKT IVVTGGEPLT WDMTVLTQRL KAENLQVHIE TSGAYPVTGA
WDWFCLSPKK NKLPVAEAYE IAHELKVIIY NKHDFIFAEE QAAKVNKNAI LFLQSEWSKK
EEMTPFIVDY VMNNPKWRVS LQTHKYLNIP
