Legends: 1, Iron-sulfur (4Fe-4S-S-AdoMet). {ECO:0000255|HAMAP-Rule:MF_00917}; 2, Magnesium. {ECO:0000255|HAMAP- Rule:MF_00917}; 3, BINDING Substrate. {ECO:0000255|HAMAP- Rule:MF_00917}; 4, BINDING S-adenosyl-L-methionine; via carbonyl oxygen. {ECO:0000255|HAMAP- Rule:MF_00917}; 5, BINDING Substrate; via carboxylate. {ECO:0000255|HAMAP-Rule:MF_00917}; 6, REGION Substrate binding. {ECO:0000255|HAMAP- Rule:MF_00917}; 7, REGION S-adenosyl-L-methionine binding. {ECO:0000255|HAMAP-Rule:MF_00917}.
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ID QUEE_HYPBU Reviewed; 235 AA.
AC A2BJ90;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 17-FEB-2016, entry version 50.
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=Archaeosine biosynthesis protein QueE {ECO:0000255|HAMAP-Rule:MF_00917};
GN Name=queE {ECO:0000255|HAMAP-Rule:MF_00917};
GN OrderedLocusNames=Hbut_0179;
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Pyrodictiaceae; Hyperthermus.
OX NCBI_TaxID=415426;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=17350933; DOI=10.1155/2007/745987;
RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A.,
RA Awayez M., She Q., Garrett R.A., Klenk H.-P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
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}.
DR EMBL; CP000493; ABM80051.1; -; Genomic_DNA.
DR ProteinModelPortal; A2BJ90; -.
DR STRING; 415426.Hbut_0179; -.
DR EnsemblBacteria; ABM80051; ABM80051; Hbut_0179.
DR KEGG; hbu:Hbut_0179; -.
DR eggNOG; arCOG02173; Archaea.
DR eggNOG; COG0602; LUCA.
DR HOGENOM; HOG000266145; -.
DR OMA; FQIDIND; -.
DR BioCyc; HBUT415426:GC56-179-MONOMER; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000002593; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-HAMAP.
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 PIRSF; PIRSF000370; QueE; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Magnesium;
KW Metal-binding; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1 235 7-carboxy-7-deazaguanine synthase.
FT /FTId=PRO_0000416216.
FT REGION 25 27 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00917}.
FT REGION 135 137 S-adenosyl-L-methionine binding.
FT {ECO:0000255|HAMAP-Rule:MF_00917}.
FT METAL 44 44 Iron-sulfur (4Fe-4S-S-AdoMet).
FT {ECO:0000255|HAMAP-Rule:MF_00917}.
FT METAL 48 48 Iron-sulfur (4Fe-4S-S-AdoMet).
FT {ECO:0000255|HAMAP-Rule:MF_00917}.
FT METAL 51 51 Iron-sulfur (4Fe-4S-S-AdoMet).
FT {ECO:0000255|HAMAP-Rule:MF_00917}.
FT METAL 53 53 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00917}.
FT BINDING 40 40 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_00917}.
FT BINDING 85 85 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_00917}.
FT BINDING 87 87 S-adenosyl-L-methionine; via carbonyl
FT oxygen. {ECO:0000255|HAMAP-
FT Rule:MF_00917}.
FT BINDING 235 235 Substrate; via carboxylate.
FT {ECO:0000255|HAMAP-Rule:MF_00917}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 16 235 ihamap:QueE [T]
FT MYHIT 39 199 ipfam:Radical_SAM [T]
SQ SEQUENCE 235 AA; 26499 MW; 15EEC793F5E850C1 CRC64;
MSRSARRKTS ALNTVLRVVE VFASIQGEGP FTGTYSVFVR LAGCNLRCPF CDTRYAWSLE
AGKPLGVEEL VEEIARYEPS LVVITGGEPL LQRHPLNSLV EGLESLGLRV QLETNGILPA
PARDEQLWRV YHVVSPKDVP VRVPGAKLHP SWVDYARATG RAWFKFLVAN EQHVREVAEY
VAKLGIPRSR VYIMPLTPEK LDMKELLELH SRIASLAVKW RLNFSPRLHL LVQLP
//
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