QUEC_PECAS
ID QUEC_PECAS Reviewed; 231 AA.
AC Q6D820;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=7-cyano-7-deazaguanine synthase;
DE EC=6.3.4.20;
DE AltName: Full=7-cyano-7-carbaguanine synthase;
DE AltName: Full=PreQ(0) synthase;
DE AltName: Full=Queuosine biosynthesis protein QueC;
GN Name=queC; OrderedLocusNames=ECA1155;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC ION, AND
RP COFACTOR.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of hypothetical protein (yp_049261.1) from Erwinia
RT carotovora subsp. atroseptica scri1043 at 2.40 A resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7-
CC deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|Ref.2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|Ref.2};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC -!- SIMILARITY: Belongs to the QueC family. {ECO:0000305}.
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DR EMBL; BX950851; CAG74065.1; -; Genomic_DNA.
DR RefSeq; WP_011092748.1; NC_004547.2.
DR PDB; 2PG3; X-ray; 2.40 A; A=1-231.
DR PDBsum; 2PG3; -.
DR AlphaFoldDB; Q6D820; -.
DR SMR; Q6D820; -.
DR STRING; 218491.ECA1155; -.
DR DNASU; 2885761; -.
DR EnsemblBacteria; CAG74065; CAG74065; ECA1155.
DR GeneID; 57207969; -.
DR KEGG; eca:ECA1155; -.
DR PATRIC; fig|218491.5.peg.1170; -.
DR eggNOG; COG0603; Bacteria.
DR HOGENOM; CLU_081854_0_0_6; -.
DR OMA; CESCMRR; -.
DR OrthoDB; 1681374at2; -.
DR UniPathway; UPA00391; -.
DR EvolutionaryTrace; Q6D820; -.
DR Proteomes; UP000007966; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Metal-binding; Nucleotide-binding;
KW Queuosine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..231
FT /note="7-cyano-7-deazaguanine synthase"
FT /id="PRO_0000246839"
FT BINDING 8..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:2PG3"
FT STRAND 26..38
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:2PG3"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:2PG3"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2PG3"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:2PG3"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2PG3"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:2PG3"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:2PG3"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:2PG3"
SQ SEQUENCE 231 AA; 25363 MW; A6AEA71C503D42A0 CRC64;
MKRAVVVFSG GQDSTTCLIQ ALQDYDDVHC ITFDYGQRHR AEIEVAQELS QKLGAAAHKV
LDVGLLNELA TSSLTRDSIP VPDYDANAQG IPNTFVPGRN ILFLTLASIY AYQVGAEAVI
TGVCETDFSG YPDCRDEFVK ALNQAIVLGI ARDIRFETPL MWLNKAETWA LADYYQQLDT
VRYHTLTCYN GIKGDGCGQC AACHLRANGL AQYQKDAATV MASLKQKVGL R
