QUEE_BACSU
ID QUEE_BACSU Reviewed; 243 AA.
AC O31677;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000303|PubMed:23194065};
DE Short=CDG synthase {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000303|PubMed:23194065};
DE EC=4.3.99.3 {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:19354300, ECO:0000269|PubMed:23194065};
DE AltName: Full=Queuosine biosynthesis protein QueE {ECO:0000255|HAMAP-Rule:MF_00917};
GN Name=queE {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000303|PubMed:14660578};
GN Synonyms=ykvL; OrderedLocusNames=BSU13740;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION IN QUEUOSINE BIOSYNTHESIS, AND GENE NAME.
RX PubMed=14660578; DOI=10.1074/jbc.m310858200;
RA Reader J.S., Metzgar D., Schimmel P., de Crecy-Lagard V.;
RT "Identification of four genes necessary for biosynthesis of the modified
RT nucleoside queuosine.";
RL J. Biol. Chem. 279:6280-6285(2004).
RN [3]
RP FUNCTION AS CDG SYNTHASE, CATALYTIC ACTIVITY, COFACTOR,
RP S-ADENOSYL-L-METHIONINE-BINDING, AND PATHWAY.
RC STRAIN=168 / ATCC 23857D;
RX PubMed=19354300; DOI=10.1021/bi900400e;
RA McCarty R.M., Somogyi A., Lin G., Jacobsen N.E., Bandarian V.;
RT "The deazapurine biosynthetic pathway revealed: in vitro enzymatic
RT synthesis of PreQ(0) from guanosine 5'-triphosphate in four steps.";
RL Biochemistry 48:3847-3852(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND REACTION MECHANISM.
RX PubMed=23194065; DOI=10.1021/bi301156w;
RA McCarty R.M., Krebs C., Bandarian V.;
RT "Spectroscopic, steady-state kinetic, and mechanistic characterization of
RT the radical SAM enzyme QueE, which catalyzes a complex cyclization reaction
RT in the biosynthesis of 7-deazapurines.";
RL Biochemistry 52:188-198(2013).
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 ECO:0000269|PubMed:14660578, ECO:0000269|PubMed:19354300,
CC ECO:0000269|PubMed:23194065}.
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 ECO:0000269|PubMed:19354300, ECO:0000269|PubMed:23194065};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:23194065, ECO:0000305|PubMed:19354300};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000269|PubMed:23194065, ECO:0000305|PubMed:19354300};
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917,
CC ECO:0000269|PubMed:19354300, ECO:0000269|PubMed:23194065};
CC Note=Binds 1 S-adenosyl-L-methionine per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00917, ECO:0000269|PubMed:19354300,
CC ECO:0000269|PubMed:23194065};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917,
CC ECO:0000269|PubMed:23194065};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for 6-carboxy-5,6,7,8-tetrahydropterin
CC {ECO:0000269|PubMed:23194065};
CC Note=kcat is 5.4 min(-1). {ECO:0000269|PubMed:23194065};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:19354300}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00917,
CC ECO:0000269|PubMed:23194065}.
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; AL009126; CAB13247.1; -; Genomic_DNA.
DR PIR; C69868; C69868.
DR RefSeq; NP_389257.1; NC_000964.3.
DR RefSeq; WP_003232460.1; NZ_JNCM01000035.1.
DR PDB; 5TGS; X-ray; 2.55 A; A/B=1-243.
DR PDB; 5TH5; X-ray; 2.41 A; A/B/C/D=1-243.
DR PDBsum; 5TGS; -.
DR PDBsum; 5TH5; -.
DR AlphaFoldDB; O31677; -.
DR SMR; O31677; -.
DR IntAct; O31677; 1.
DR STRING; 224308.BSU13740; -.
DR jPOST; O31677; -.
DR PaxDb; O31677; -.
DR PRIDE; O31677; -.
DR DNASU; 939290; -.
DR EnsemblBacteria; CAB13247; CAB13247; BSU_13740.
DR GeneID; 939290; -.
DR KEGG; bsu:BSU13740; -.
DR PATRIC; fig|224308.179.peg.1491; -.
DR eggNOG; COG0602; Bacteria.
DR InParanoid; O31677; -.
DR OMA; MFVRTGG; -.
DR PhylomeDB; O31677; -.
DR BioCyc; BSUB:BSU13740-MON; -.
DR BioCyc; MetaCyc:BSU13740-MON; -.
DR BRENDA; 4.3.99.3; 658.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
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; IPR017742; Deazaguanine_synth.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000370; QueE; 1.
DR SFLD; SFLDF00300; 7-carboxy-7-deazaguanine_synth; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR TIGRFAMs; TIGR03365; Bsubt_queE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Lyase; Magnesium; Metal-binding;
KW Queuosine biosynthesis; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..243
FT /note="7-carboxy-7-deazaguanine synthase"
FT /id="PRO_0000392071"
FT DOMAIN 21..239
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 15..17
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 34
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="[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 41
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 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT BINDING 127..129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00917"
FT STRAND 5..15
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:5TH5"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5TH5"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:5TH5"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:5TH5"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5TH5"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5TH5"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:5TH5"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5TH5"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:5TH5"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 199..218
FT /evidence="ECO:0007829|PDB:5TH5"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:5TH5"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:5TH5"
SQ SEQUENCE 243 AA; 27122 MW; 8F44E27D21A7B1FD CRC64;
MAKGIPVLEI FGPTIQGEGM VIGQKTMFVR TAGCDYSCSW CDSAFTWDGS AKKDIRWMTA
EEIFAELKDI GGDAFSHVTI SGGNPALLKQ LDAFIELLKE NNIRAALETQ GTVYQDWFTL
IDDLTISPKP PSSKMVTNFQ KLDHILTSLQ ENDRQHAVSL KVVIFNDEDL EFAKTVHKRY
PGIPFYLQVG NDDVHTTDDQ SLIAHLLGKY EALVDKVAVD AELNLVRVLP QLHTLLWGNK
RGV
