QUEC_STAAW
ID QUEC_STAAW Reviewed; 222 AA.
AC Q7A1I5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=7-cyano-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE EC=6.3.4.20 {ECO:0000255|HAMAP-Rule:MF_01633};
DE AltName: Full=7-cyano-7-carbaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE AltName: Full=PreQ(0) synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE AltName: Full=Queuosine biosynthesis protein QueC {ECO:0000255|HAMAP-Rule:MF_01633};
GN Name=queC {ECO:0000255|HAMAP-Rule:MF_01633}; OrderedLocusNames=MW0674;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7-
CC deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
CC {ECO:0000255|HAMAP-Rule:MF_01633}.
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:0000255|HAMAP-Rule:MF_01633};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01633};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01633};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01633}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01633}.
CC -!- SIMILARITY: Belongs to the QueC family. {ECO:0000255|HAMAP-
CC Rule:MF_01633}.
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DR EMBL; BA000033; BAB94539.1; -; Genomic_DNA.
DR RefSeq; WP_000446724.1; NC_003923.1.
DR AlphaFoldDB; Q7A1I5; -.
DR SMR; Q7A1I5; -.
DR EnsemblBacteria; BAB94539; BAB94539; BAB94539.
DR KEGG; sam:MW0674; -.
DR HOGENOM; CLU_081854_0_0_9; -.
DR OMA; CESCMRR; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000000418; 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; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding; Ligase; Metal-binding; Nucleotide-binding;
KW Queuosine biosynthesis; Zinc.
FT CHAIN 1..222
FT /note="7-cyano-7-deazaguanine synthase"
FT /id="PRO_0000246933"
FT BINDING 14..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
SQ SEQUENCE 222 AA; 24887 MW; 00D0277C77C8DA6D CRC64;
MESVLNNEKA IVVFSGGQDS TTCLFYAKKH FKEVELVTFN YGQRHDTEIE VAKQIAQDQG
MKHHVLDMSL LSQLTPNALT QHDMEITNNE DGIPNTFVPA RNLLFLSFAG ALAYQIGAKH
IITGVCETDF SGYPDCRDSF IKSMNVTLSL AMDKDFVIHT PLMWLNKAET WKLSDELEVL
DYIRTKTLTC YNGIIGDGCG ECPACHLRQR GLNQYLESKG AL