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 28-FEB-2018, entry version 76. 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}; GN OrderedLocusNames=GSU1721; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Proteobacteria; 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., RA Van Aken S.E., 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- CC carboxy-7-deazaguanine (CDG), a step common to the biosynthetic CC pathways of all 7-deazapurine-containing compounds. CC {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- CATALYTIC ACTIVITY: 6-carboxy-5,6,7,8-tetrahydropterin = 7- CC carboxy-7-carbaguanine + NH(3). {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. CC {ECO:0000255|HAMAP-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 ProteinModelPortal; Q74CF3; -. DR STRING; 243231.GSU1721; -. DR DNASU; 2687051; -. DR EnsemblBacteria; AAR35098; AAR35098; GSU1721. DR GeneID; 2687051; -. DR KEGG; gsu:GSU1721; -. DR PATRIC; fig|243231.5.peg.1762; -. DR eggNOG; ENOG4107WPW; Bacteria. DR eggNOG; COG0602; LUCA. DR HOGENOM; HOG000266147; -. DR InParanoid; Q74CF3; -. DR KO; K10026; -. DR OMA; VIPQTHK; -. DR OrthoDB; POG091H00E2; -. DR BioCyc; GSUL243231:G1G0I-1925-MONOMER; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000577; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-KW. 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 SFLD; SFLDS00029; Radical_SAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Magnesium; KW Metal-binding; Queuosine biosynthesis; Reference proteome; KW S-adenosyl-L-methionine. FT CHAIN 1 250 7-carboxy-7-deazaguanine synthase. FT /FTId=PRO_0000416205. FT REGION 15 17 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT METAL 34 34 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 38 38 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 41 41 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 43 43 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 30 30 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 96 96 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 98 98 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT 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 //