QUEC1_RHILO
ID QUEC1_RHILO Reviewed; 232 AA.
AC Q98AZ0; Q8KGJ8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=7-cyano-7-deazaguanine synthase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01633};
DE AltName: Full=PreQ(0) synthase 1 {ECO:0000255|HAMAP-Rule:MF_01633};
DE AltName: Full=Queuosine biosynthesis protein QueC 1 {ECO:0000255|HAMAP-Rule:MF_01633};
GN Name=queC1 {ECO:0000255|HAMAP-Rule:MF_01633}; OrderedLocusNames=mll5798;
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; AL672115; CAD31242.1; -; Genomic_DNA.
DR EMBL; BA000012; BAB52182.1; -; Genomic_DNA.
DR RefSeq; WP_010913518.1; NC_002678.2.
DR AlphaFoldDB; Q98AZ0; -.
DR SMR; Q98AZ0; -.
DR STRING; 266835.14025582; -.
DR EnsemblBacteria; BAB52182; BAB52182; BAB52182.
DR KEGG; mlo:mll5798; -.
DR PATRIC; fig|266835.9.peg.4613; -.
DR eggNOG; COG0603; Bacteria.
DR HOGENOM; CLU_081854_1_0_5; -.
DR OMA; QDPIKYV; -.
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..232
FT /note="7-cyano-7-deazaguanine synthase 1"
FT /id="PRO_0000246900"
FT BINDING 7..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 196
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 CONFLICT 53
FT /note="A -> G (in Ref. 1; CAD31242)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="K -> Q (in Ref. 1; CAD31242)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="E -> G (in Ref. 1; CAD31242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 25125 MW; 19FEE72A3FDC560F CRC64;
MNALVICSGG LDSVSLAHKV ATEQKLIGLL SFDYGQRHKK ELGFAAICAK RLAVPHQIVD
IRDVGRNLSG SALTDNVDVP DGHYAEDSMR ITVVPNRNAI MLAIAFGVAA AKKADAVATA
VHGGDHFIYP DCRPAFIDAF QTMQNHALAG YADIRLYAPY VNMSKADIVS EGAKYATPFE
ATWSCYKGGA RHCGRCGTCV ERREAFDLAG ITDPTDYEDA DFWLHAIQTR SA
