(data stored in SCRATCH zone)

SWISSPROT: C8U2D1_ECO10

ID   C8U2D1_ECO10            Unreviewed;       231 AA.
AC   C8U2D1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=7-cyano-7-deazaguanine synthase {ECO:0000256|HAMAP-Rule:MF_01633, ECO:0000256|SAAS:SAAS00735394};
DE            EC=6.3.4.20 {ECO:0000256|HAMAP-Rule:MF_01633, ECO:0000256|SAAS:SAAS00695393};
DE   AltName: Full=7-cyano-7-carbaguanine synthase {ECO:0000256|HAMAP-Rule:MF_01633};
DE   AltName: Full=PreQ(0) synthase {ECO:0000256|HAMAP-Rule:MF_01633};
DE   AltName: Full=Queuosine biosynthesis protein QueC {ECO:0000256|HAMAP-Rule:MF_01633};
GN   Name=ybaX {ECO:0000313|EMBL:BAI29289.1};
GN   Synonyms=queC {ECO:0000256|HAMAP-Rule:MF_01633};
GN   OrderedLocusNames=ECO103_0421 {ECO:0000313|EMBL:BAI29289.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29289.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29289.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7-
CC       deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
CC       {ECO:0000256|HAMAP-Rule:MF_01633, ECO:0000256|SAAS:SAAS00695390}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-
CC         deazaguanine + ADP + H(+) + H2O + phosphate;
CC         Xref=Rhea:RHEA:27982, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:45075, ChEBI:CHEBI:61036, ChEBI:CHEBI:456216;
CC         EC=6.3.4.20; Evidence={ECO:0000256|HAMAP-Rule:MF_01633,
CC         ECO:0000256|SAAS:SAAS01119635};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01633};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01633};
CC   -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01633, ECO:0000256|SAAS:SAAS00695391}.
CC   -!- SIMILARITY: Belongs to the QueC family. {ECO:0000256|HAMAP-
CC       Rule:MF_01633, ECO:0000256|SAAS:SAAS00695396}.
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DR   EMBL; AP010958; BAI29289.1; -; Genomic_DNA.
DR   RefSeq; WP_000817229.1; NC_013353.1.
DR   SMR; C8U2D1; -.
DR   EnsemblBacteria; BAI29289; BAI29289; ECO103_0421.
DR   KEGG; eoh:ECO103_0421; -.
DR   HOGENOM; HOG000110563; -.
DR   KO; K06920; -.
DR   OMA; VWVPARN; -.
DR   BioCyc; ECOL585395:ECO103_RS02205-MONOMER; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000000959; 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;
DR   PRODOM; C8U2D1.
DR   SWISS-2DPAGE; C8U2D1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01633,
KW   ECO:0000256|SAAS:SAAS00430050};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01633,
KW   ECO:0000256|SAAS:SAAS00430175};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01633,
KW   ECO:0000256|SAAS:SAAS00695387};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01633,
KW   ECO:0000256|SAAS:SAAS00430040};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01633};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01633, ECO:0000256|SAAS:SAAS00695377}.
FT   NP_BIND       8     18       ATP. {ECO:0000256|HAMAP-Rule:MF_01633}.
FT   METAL       188    188       Zinc. {ECO:0000256|HAMAP-Rule:MF_01633}.
FT   METAL       197    197       Zinc. {ECO:0000256|HAMAP-Rule:MF_01633}.
FT   METAL       200    200       Zinc. {ECO:0000256|HAMAP-Rule:MF_01633}.
FT   METAL       203    203       Zinc. {ECO:0000256|HAMAP-Rule:MF_01633}.
SQ   SEQUENCE   231 AA;  25480 MW;  6511CDD03E6E3E3D CRC64;
     MKRAVVVFSG GQDSTTCLVQ ALQQYDEVHC VTFDYGQRHR AEIDVARELA LKLGARAHKV
     LDVTLLNELA VSSLTRDSIP VPDYEPEADG IPNTFVPGRN ILFLTLAAIY AYQVKAEAVI
     TGVCETDFSG YPDCRDEFVK ALNHAVSLGM AKDIRFETPL MWIDKAETWA LADYYGKLDL
     VRNETLTCYN GIKGDGCGHC AACNLRANGL NHYLADKPTV MAAMKQKTGL R
//

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