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Database: UniProt
Entry: R6DJQ8_9CLOT
LinkDB: R6DJQ8_9CLOT
Original site: R6DJQ8_9CLOT 
ID   R6DJQ8_9CLOT            Unreviewed;       220 AA.
AC   R6DJQ8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000256|HAMAP-Rule:MF_00917};
DE            Short=CDG synthase {ECO:0000256|HAMAP-Rule:MF_00917};
DE            EC=4.3.99.3 {ECO:0000256|HAMAP-Rule:MF_00917};
DE   AltName: Full=Queuosine biosynthesis protein QueE {ECO:0000256|HAMAP-Rule:MF_00917};
GN   Name=queE {ECO:0000256|HAMAP-Rule:MF_00917};
GN   ORFNames=BN547_01997 {ECO:0000313|EMBL:CDA87860.1};
OS   Clostridium sp. CAG:230.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262782 {ECO:0000313|EMBL:CDA87860.1, ECO:0000313|Proteomes:UP000017961};
RN   [1] {ECO:0000313|EMBL:CDA87860.1, ECO:0000313|Proteomes:UP000017961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:230 {ECO:0000313|Proteomes:UP000017961};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00917};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
CC   -!- COFACTOR:
CC       Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
CC       Note=Binds 1 S-adenosyl-L-methionine per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00917};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00917};
CC   -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00917}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00917}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7-
CC       deazaguanine synthase family. {ECO:0000256|HAMAP-Rule:MF_00917}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00917}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDA87860.1}.
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DR   EMBL; CBCQ010000183; CDA87860.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6DJQ8; -.
DR   STRING; 1262782.BN547_01997; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000017961; Unassembled WGS sequence.
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; IPR023868; 7-CO-7-deazaGua_synth_put_Clo.
DR   InterPro; IPR024924; 7-CO-7-deazaguanine_synth-like.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR03963; rSAM_QueE_Clost; 1.
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   PIRSF; PIRSF000370; QueE; 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 {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00917};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00917};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00917};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00917};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00917};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00917}; Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017961};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00917}.
FT   DOMAIN          19..215
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         13..15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT   BINDING         32
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT   BINDING         36
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT   BINDING         38..40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT   BINDING         39
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
SQ   SEQUENCE   220 AA;  24941 MW;  5686446809B5A897 CRC64;
     MNTYKVVEIF ESINGEGMKA GELSVFVRLC GCNLHCSYCD TSWANEKDAP YQEMTARQIV
     QKAEAYGTKN VTLTGGEPLL AEHVLELLEA LSEKFCVEIE TNGSIALDPF CKKDRKVIFT
     MDYKLKGSGM EEQMCLSNFA LLQRDDTVKF VVSDQTDLER AYEIEQKYAL GQKCHVLISP
     VFGKIIPADM VAFMMEKKWV TARMQIQMHK VIWDPQARGV
//
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