QUEE_DESVH
ID QUEE_DESVH Reviewed; 216 AA.
AC Q728E5;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=DVU_2658;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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; AE017285; AAS97130.1; -; Genomic_DNA.
DR RefSeq; WP_010939927.1; NC_002937.3.
DR RefSeq; YP_011870.1; NC_002937.3.
DR AlphaFoldDB; Q728E5; -.
DR SMR; Q728E5; -.
DR STRING; 882.DVU_2658; -.
DR PaxDb; Q728E5; -.
DR EnsemblBacteria; AAS97130; AAS97130; DVU_2658.
DR KEGG; dvu:DVU_2658; -.
DR PATRIC; fig|882.5.peg.2402; -.
DR eggNOG; COG0602; Bacteria.
DR HOGENOM; CLU_066739_0_1_7; -.
DR OMA; CDVKESW; -.
DR PhylomeDB; Q728E5; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000002194; 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; 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 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..216
FT /note="7-carboxy-7-deazaguanine synthase"
FT /id="PRO_0000416203"
FT DOMAIN 18..216
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 12..14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00917"
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 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 BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 136..138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 176..179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
SQ SEQUENCE 216 AA; 23535 MW; 7D6C339FF97ED445 CRC64;
MTYRVKEIFH TLQGEGMRAG RAAVFCRFSG CNLWTGWAQD RPAAVCPFCD TDFVGTDGPG
GGVFEDAATL AAAILAAFPY KTGEGYRPYV VFTGGEPALQ LDRPLIDILH AHGCEVAIET
NGTVRLPEGI DWVTVSPKAG TRLAVTSGDE LKLVWPQQGI CPESYESLAF TYLLMQPRDG
LGDAGRGDAE SEAVRWCLAH PRWRLCLQTH KYLGIP
