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QUEE_RICPR
ID   QUEE_RICPR              Reviewed;         234 AA.
AC   Q9ZCV2;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=RP607;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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}.
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DR   EMBL; AJ235272; CAA15051.1; -; Genomic_DNA.
DR   PIR; A71666; A71666.
DR   RefSeq; NP_220975.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCV2; -.
DR   SMR; Q9ZCV2; -.
DR   STRING; 272947.RP607; -.
DR   EnsemblBacteria; CAA15051; CAA15051; CAA15051.
DR   KEGG; rpr:RP607; -.
DR   PATRIC; fig|272947.5.peg.626; -.
DR   eggNOG; COG0602; Bacteria.
DR   HOGENOM; CLU_066739_2_3_5; -.
DR   OMA; CDVKESW; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000002480; 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   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.
DR   SFLD; SFLDS00029; Radical_SAM; 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..234
FT                   /note="7-carboxy-7-deazaguanine synthase"
FT                   /id="PRO_0000416213"
FT   DOMAIN          42..234
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         36..38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT   BINDING         55
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         59
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         62
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         64
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT   BINDING         102
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT   BINDING         144..146
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT   BINDING         195..198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
SQ   SEQUENCE   234 AA;  26247 MW;  1BC9DAEE2E04C64B CRC64;
     MNQRINSYKM FGHNPKRSIL SGDGTKLEVQ SIFKTIQGEG IFVGYPSIFI RLGGCNLACN
     FCDTEFEDFK LIDIDQILNK VKNLSLNSKN AKTINLVVIT GGEPMRQPIG LLCQKLLDQD
     FKVQIETNGT LYRSLPKEVF IVCSPKVGKT GYNKIREDLL PQISAVKFII SKNIVEYSII
     PEVGQSAYDI PVFVQSMDQN DKRLNNENNE LAVKLALESG ARLSLQTHKF LGIE
 
 
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