QUEC_BACSU
ID QUEC_BACSU Reviewed; 219 AA.
AC O31675;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=7-cyano-7-deazaguanine synthase;
DE EC=6.3.4.20 {ECO:0000269|PubMed:19354300};
DE AltName: Full=7-cyano-7-carbaguanine synthase;
DE AltName: Full=PreQ(0) synthase;
DE AltName: Full=Queuosine biosynthesis protein QueC;
GN Name=queC; Synonyms=ykvJ; OrderedLocusNames=BSU13720;
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 PREQ(0) SYNTHASE, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC STRAIN=168;
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 X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND ATP
RP ANALOG, COFACTOR, AND SUBUNIT.
RX PubMed=18491386; DOI=10.1002/prot.22098;
RA Cicmil N., Huang R.H.;
RT "Crystal structure of QueC from Bacillus subtilis: an enzyme involved in
RT preQ1 biosynthesis.";
RL Proteins 72:1084-1088(2008).
CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7-
CC deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Uses ammonia as
CC nitrogen donor. {ECO:0000269|PubMed:14660578,
CC ECO:0000269|PubMed:19354300}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-
CC deazaguanine + ADP + H(+) + H2O + phosphate; Xref=Rhea:RHEA:27982,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:45075,
CC ChEBI:CHEBI:61036, ChEBI:CHEBI:456216; EC=6.3.4.20;
CC Evidence={ECO:0000269|PubMed:19354300};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:18491386, ECO:0000269|PubMed:19354300};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18491386,
CC ECO:0000269|PubMed:19354300};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC {ECO:0000269|PubMed:19354300}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18491386}.
CC -!- SIMILARITY: Belongs to the QueC family. {ECO:0000305}.
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DR EMBL; AL009126; CAB13245.1; -; Genomic_DNA.
DR PIR; A69868; A69868.
DR RefSeq; NP_389255.1; NC_000964.3.
DR RefSeq; WP_003245417.1; NZ_JNCM01000035.1.
DR PDB; 3BL5; X-ray; 2.95 A; A/B/C/D/E/F=1-219.
DR PDBsum; 3BL5; -.
DR AlphaFoldDB; O31675; -.
DR SMR; O31675; -.
DR STRING; 224308.BSU13720; -.
DR PaxDb; O31675; -.
DR PRIDE; O31675; -.
DR EnsemblBacteria; CAB13245; CAB13245; BSU_13720.
DR GeneID; 939292; -.
DR KEGG; bsu:BSU13720; -.
DR PATRIC; fig|224308.179.peg.1489; -.
DR eggNOG; COG0603; Bacteria.
DR InParanoid; O31675; -.
DR OMA; CESCMRR; -.
DR PhylomeDB; O31675; -.
DR BioCyc; BSUB:BSU13720-MON; -.
DR BioCyc; MetaCyc:BSU13720-MON; -.
DR BRENDA; 6.3.4.20; 658.
DR UniPathway; UPA00391; -.
DR EvolutionaryTrace; O31675; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
DR CDD; cd01995; ExsB; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01633; QueC; 1.
DR InterPro; IPR018317; QueC.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR42914; PTHR42914; 1.
DR Pfam; PF06508; QueC; 1.
DR PIRSF; PIRSF006293; ExsB; 1.
DR TIGRFAMs; TIGR00364; TIGR00364; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Metal-binding; Nucleotide-binding;
KW Queuosine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..219
FT /note="7-cyano-7-deazaguanine synthase"
FT /id="PRO_0000246801"
FT BINDING 10..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18491386"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18491386"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18491386"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18491386"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18491386"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3BL5"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:3BL5"
FT STRAND 28..38
FT /evidence="ECO:0007829|PDB:3BL5"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:3BL5"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3BL5"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:3BL5"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3BL5"
FT HELIX 97..112
FT /evidence="ECO:0007829|PDB:3BL5"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3BL5"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3BL5"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:3BL5"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3BL5"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:3BL5"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:3BL5"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:3BL5"
FT HELIX 199..213
FT /evidence="ECO:0007829|PDB:3BL5"
SQ SEQUENCE 219 AA; 24529 MW; 146535A4A91EB894 CRC64;
MKKEKAIVVF SGGQDSTTCL LWALKEFEEV ETVTFHYNQR HSQEVEVAKS IAEKLGVKNH
LLDMSLLNQL APNALTRNDI EIEVKDGELP STFVPGRNLV FLSFASILAY QIGARHIITG
VCETDFSGYP DCRDEFVKSC NVTVNLAMEK PFVIHTPLMW LNKAETWKLA DELGALDFVK
NNTLTCYNGI IADGCGECPA CHLRSKGYEE YMVMKGERA
