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QUEE_KORVE
ID   QUEE_KORVE              Reviewed;         226 AA.
AC   Q1IHK7;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Acid345_4643;
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Candidatus Koribacter.
OX   NCBI_TaxID=204669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000360; ABF43643.1; -; Genomic_DNA.
DR   RefSeq; WP_011525440.1; NC_008009.1.
DR   AlphaFoldDB; Q1IHK7; -.
DR   SMR; Q1IHK7; -.
DR   STRING; 204669.Acid345_4643; -.
DR   EnsemblBacteria; ABF43643; ABF43643; Acid345_4643.
DR   KEGG; aba:Acid345_4643; -.
DR   eggNOG; COG0602; Bacteria.
DR   HOGENOM; CLU_066739_2_0_0; -.
DR   OMA; CDTEYAF; -.
DR   OrthoDB; 1141206at2; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000002432; 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..226
FT                   /note="7-carboxy-7-deazaguanine synthase"
FT                   /id="PRO_0000416207"
FT   DOMAIN          16..221
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         10..12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT   BINDING         29
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         33
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         36
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         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT   BINDING         71
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
SQ   SEQUENCE   226 AA;  25356 MW;  253E2F94D975674F CRC64;
     MQITEIYRSL QGESSYTGIP CIFVRLTACN LRCAWCDSEY TFKGGRKMSE DEIFAEVQKL
     APGGLVEITG GEPLLQEREL VPFMERLVAS GYKVLIETSG ERPLANVPQD VVKIVDVKCP
     ASGEGGSFRI ENLDALTPHD EIKFVISDRA DYEFAREFTR QHGLENKVSS VIFSPAFRKD
     ARGTRDASHC LVDPQDLANW VLEDQLDVRL GLQTHKFIWT PETKGV
 
 
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