QUEC2_RHILO
ID QUEC2_RHILO Reviewed; 245 AA.
AC Q98AM3; Q8KGN5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=7-cyano-7-deazaguanine synthase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01633};
DE AltName: Full=PreQ(0) synthase 2 {ECO:0000255|HAMAP-Rule:MF_01633};
DE AltName: Full=Queuosine biosynthesis protein QueC 2 {ECO:0000255|HAMAP-Rule:MF_01633};
GN Name=queC2 {ECO:0000255|HAMAP-Rule:MF_01633}; OrderedLocusNames=mll5936;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R7A;
RX PubMed=12003951; DOI=10.1128/jb.184.11.3086-3095.2002;
RA Sullivan J.T., Trzebiatowski J.R., Cruickshank R.W., Gouzy J., Brown S.D.,
RA Elliot R.M., Fleetwood D.J., McCallum N.G., Rossbach U., Stuart G.S.,
RA Weaver J.E., Webby R.J., de Bruijn F.J., Ronson C.W.;
RT "Comparative sequence analysis of the symbiosis island of Mesorhizobium
RT loti strain R7A.";
RL J. Bacteriol. 184:3086-3095(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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 -!- SIMILARITY: Belongs to the QueC family. {ECO:0000255|HAMAP-
CC Rule:MF_01633}.
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DR EMBL; AL672114; CAD31298.1; -; Genomic_DNA.
DR EMBL; BA000012; BAB52299.1; -; Genomic_DNA.
DR RefSeq; WP_010913630.1; NC_002678.2.
DR AlphaFoldDB; Q98AM3; -.
DR SMR; Q98AM3; -.
DR STRING; 266835.14025699; -.
DR EnsemblBacteria; BAB52299; BAB52299; BAB52299.
DR KEGG; mlo:mll5936; -.
DR eggNOG; COG0603; Bacteria.
DR HOGENOM; CLU_081854_0_0_5; -.
DR OMA; ICEGSHT; -.
DR OrthoDB; 1681374at2; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000000552; 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..245
FT /note="7-cyano-7-deazaguanine synthase 2"
FT /id="PRO_0000246901"
FT BINDING 12..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT CONFLICT 55
FT /note="E -> G (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="G -> E (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="G -> D (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="P -> T (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="L -> I (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 123..124
FT /note="LS -> MG (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="A -> S (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="I -> M (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 161..164
FT /note="KRFI -> THLV (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="H -> R (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="D -> G (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> V (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="S -> C (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="T -> A (in Ref. 1; CAD31298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 27324 MW; A50EB2627A01C19B CRC64;
MQRDPGTALV LFSGGQDSTT CLAWALENFE RVETIGFDYG QRHRIELDVR PYLLERIRTD
FPAWRGRLGG DHMIDMAVLG QISDTALTRG VEVALNANGL PNTFVPGRNL LFLGFAAALA
YRLSAKHLVI GVAETDRFSY PDCRDDAVKA IQLALNLGME KRFIIHTPLM HRDKAQTWAL
ADWLGGEALV KLICEGSHTC YSGDREHRHS WGFGCGTCIE CNLRAAGWEQ FRSCKEAPVT
AHEMT
