(data stored in SCRATCH zone)

SWISSPROT: Q146Z5_PARXL

ID   Q146Z5_PARXL            Unreviewed;       210 AA.
AC   Q146Z5;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 74.
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=Bxe_A4406 {ECO:0000313|EMBL:ABE28594.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28594.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28594.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28594.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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: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;
CC         EC=4.3.99.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         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.
CC       {ECO:0000256|HAMAP-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}.
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DR   EMBL; CP000270; ABE28594.1; -; Genomic_DNA.
DR   RefSeq; WP_011486452.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4406; -.
DR   EnsemblBacteria; ABE28594; ABE28594; Bxe_A4406.
DR   GeneID; 4005130; -.
DR   KEGG; bxb:DR64_2081; -.
DR   KEGG; bxe:Bxe_A4406; -.
DR   PATRIC; fig|266265.5.peg.57; -.
DR   eggNOG; ENOG4105EIZ; Bacteria.
DR   eggNOG; COG0602; LUCA.
DR   HOGENOM; HOG000266142; -.
DR   KO; K10026; -.
DR   OMA; CDVKESW; -.
DR   OrthoDB; 1141206at2; -.
DR   BioCyc; BXEN266265:BXE_RS00280-MONOMER; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000001817; Chromosome 1.
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   Pfam; PF04055; Radical_SAM; 1.
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.
PE   3: Inferred from homology;
DR   PRODOM; Q146Z5.
DR   SWISS-2DPAGE; Q146Z5.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00917};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00917};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00917};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00917};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00917};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00917};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00917}.
FT   DOMAIN       46    125       Radical_SAM. {ECO:0000259|Pfam:PF04055}.
FT   REGION       12     14       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00917}.
FT   REGION       48     50       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00917}.
FT   REGION      133    135       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00917}.
FT   REGION      173    176       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00917}.
FT   METAL        31     31       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00917}.
FT   METAL        46     46       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00917}.
FT   METAL        49     49       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00917}.
FT   METAL        51     51       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00917}.
FT   BINDING      27     27       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00917}.
FT   BINDING      90     90       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00917}.
FT   BINDING      92     92       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00917}.
FT   BINDING     210    210       Substrate; via carboxylate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00917}.
SQ   SEQUENCE   210 AA;  23591 MW;  8DF31367D8B74BD7 CRC64;
     MTYAVKEIFY TLQGEGANAG RPAVFCRFAG CNLWSGREED RAEAVCRFCD TDFVGTDGEN
     GGKYRTAEDL VRMIASQWPQ GEGERFVVCT GGEPMLQIDQ PLVDALHAAG FEIAIETNGS
     LPVLETIDWI CVSPKADAPL VVTKGNELKV VIPQDNQRLS EYAKLDFEYF LVQPMDGPSR
     EINTRLAIDW CKRHPQWRLS MQTHKYLNIP
//

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