QUEE_BURM1
ID QUEE_BURM1 Reviewed; 210 AA.
AC A0A0H3KB22;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000303|PubMed:24362703};
DE Short=CDG synthase {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000303|PubMed:24362703};
DE EC=4.3.99.3 {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703};
DE AltName: Full=Queuosine biosynthesis protein QueE {ECO:0000255|HAMAP-Rule:MF_00917};
GN Name=queE {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000303|PubMed:24362703};
GN OrderedLocusNames=Bmul_3115 {ECO:0000312|EMBL:ABX16799.1},
GN BMULJ_00116 {ECO:0000312|EMBL:BAG42094.1};
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEXES WITH IRON-SULFUR
RP (4FE-4S); SAM; 6-CARBOXYPTERIN; 6-CARBOXY-5,6,7,8-TETRAHYDROPTERIN;
RP 7-CARBOXY-7-DEAZAGUANINE AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, PATHWAY, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=24362703; DOI=10.1038/nchembio.1426;
RA Dowling D.P., Bruender N.A., Young A.P., McCarty R.M., Bandarian V.,
RA Drennan C.L.;
RT "Radical SAM enzyme QueE defines a new minimal core fold and metal-
RT dependent mechanism.";
RL Nat. Chem. Biol. 10:106-112(2014).
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 ECO:0000269|PubMed:24362703}.
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 ECO:0000269|PubMed:24362703};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917,
CC ECO:0000269|PubMed:24362703};
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, ECO:0000269|PubMed:24362703};
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917,
CC ECO:0000269|PubMed:24362703};
CC Note=Binds 1 S-adenosyl-L-methionine per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00917, ECO:0000269|PubMed:24362703};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917,
CC ECO:0000269|PubMed:24362703};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000305|PubMed:24362703}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00917,
CC ECO:0000269|PubMed:24362703}.
CC -!- INTERACTION:
CC A0A0H3KB22; A0A0H3KB22: queE; NbExp=2; IntAct=EBI-16224608, EBI-16224608;
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; CP000868; ABX16799.1; -; Genomic_DNA.
DR EMBL; AP009385; BAG42094.1; -; Genomic_DNA.
DR RefSeq; WP_012214363.1; NC_010804.1.
DR PDB; 4NJG; X-ray; 2.60 A; A/B=1-210.
DR PDB; 4NJH; X-ray; 1.90 A; A/B=1-210.
DR PDB; 4NJI; X-ray; 2.20 A; A/B=1-210.
DR PDB; 4NJJ; X-ray; 2.70 A; A/B=1-210.
DR PDB; 4NJK; X-ray; 1.91 A; A/B=1-210.
DR PDBsum; 4NJG; -.
DR PDBsum; 4NJH; -.
DR PDBsum; 4NJI; -.
DR PDBsum; 4NJJ; -.
DR PDBsum; 4NJK; -.
DR AlphaFoldDB; A0A0H3KB22; -.
DR SMR; A0A0H3KB22; -.
DR STRING; 395019.Bmul_3115; -.
DR EnsemblBacteria; BAG42094; BAG42094; BMULJ_00116.
DR KEGG; bmj:BMULJ_00116; -.
DR KEGG; bmu:Bmul_3115; -.
DR eggNOG; COG0602; Bacteria.
DR HOGENOM; CLU_066739_0_1_4; -.
DR OMA; CDVKESW; -.
DR BRENDA; 4.3.99.3; 8177.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000008815; Chromosome 1.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
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; IPR030977; QueE_Cx14CxxC.
DR InterPro; IPR007197; rSAM.
DR PIRSF; PIRSF000370; QueE; 1.
DR SFLD; SFLDF00376; 7-carboxy-7-deazaguanine_synth; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR TIGRFAMs; TIGR04508; queE_Cx14CxxC; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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_0000435286"
FT DOMAIN 18..210
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 12..14
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24362703"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24362703"
FT BINDING 31
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 ECO:0000269|PubMed:24362703"
FT BINDING 46
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 ECO:0000269|PubMed:24362703"
FT BINDING 48..50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24362703"
FT BINDING 49
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 ECO:0000269|PubMed:24362703"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24362703"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24362703"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24362703"
FT BINDING 133..135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24362703"
FT BINDING 173..176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24362703"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24362703"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:4NJH"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:4NJH"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:4NJH"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:4NJH"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4NJH"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:4NJH"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:4NJH"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:4NJH"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4NJH"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:4NJH"
SQ SEQUENCE 210 AA; 23148 MW; FD3B66CFDFC19922 CRC64;
MTYAVKEIFY TLQGEGANAG RPAVFCRFAG CNLWSGREED RAQAVCRFCD TDFVGTDGEN
GGKFKDADAL VATIAGLWPA GEAHRFVVCT GGEPMLQLDQ PLVDALHAAG FGIAIETNGS
LPVLESIDWI CVSPKADAPL VVTKGNELKV VIPQDNQRLA DYAKLDFEYF LVQPMDGPSR
DLNTKLAIDW CKRHPQWRLS MQTHKYLNIP
