ID QUEE_GEOSL Reviewed; 250 AA. AC Q74CF3; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 03-MAY-2023, entry version 91. 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=GSU1721; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Pseudomonadota; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=243231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51573 / DSM 12127 / PCA; RX PubMed=14671304; DOI=10.1126/science.1088727; RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E., RA Lovley D.R., Fraser C.M.; RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface RT environments."; RL Science 302:1967-1969(2003). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017180; AAR35098.1; -; Genomic_DNA. DR RefSeq; NP_952771.1; NC_002939.5. DR RefSeq; WP_010942366.1; NC_002939.5. DR AlphaFoldDB; Q74CF3; -. DR SMR; Q74CF3; -. DR STRING; 243231.GSU1721; -. DR DNASU; 2687051; -. DR EnsemblBacteria; AAR35098; AAR35098; GSU1721. DR KEGG; gsu:GSU1721; -. DR PATRIC; fig|243231.5.peg.1762; -. DR eggNOG; COG0602; Bacteria. DR HOGENOM; CLU_066739_1_0_7; -. DR InParanoid; Q74CF3; -. DR OMA; YLESNMT; -. DR OrthoDB; 9792276at2; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000577; 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 CDD; cd01335; Radical_SAM; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 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 PANTHER; PTHR42836; 7-CARBOXY-7-DEAZAGUANINE SYNTHASE; 1. DR PANTHER; PTHR42836:SF1; 7-CARBOXY-7-DEAZAGUANINE SYNTHASE; 1. DR Pfam; PF13353; Fer4_12; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 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..250 FT /note="7-carboxy-7-deazaguanine synthase" FT /id="PRO_0000416205" FT DOMAIN 21..250 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 15..17 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917" FT BINDING 30 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917" FT BINDING 34 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 38 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 41 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 43 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917" FT BINDING 96 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917" FT BINDING 98 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917" SQ SEQUENCE 250 AA; 27879 MW; 3BED339ECD30FD30 CRC64; MSKPGAELEE VFSSVQGEGM LIGLRQVFIR FRGCNLTCDY CDTPAGTPAE PCRIEQTPGR RDFVPADNPV SLDRVAALVE GWQRGWPGVH DSISITGGEP LLRHDILMQW LPVLREHLPV YLETNGVMHA ALGLVINHVD IIGMDIKIPS TSGCTDLWDD HRQFLEIANT RRAFIKIVVG EETEDWEITR ASEIIAGVNR DIPLILQPVT RAGDTLGIKP VKALELQELA CRYLAEVRII PQTHRFMGQL //