(data stored in ACNUC7421 zone)

SWISSPROT: D6XV20_BACIE

ID   D6XV20_BACIE            Unreviewed;       135 AA.
AC   D6XV20;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000256|HAMAP-Rule:MF_00818, ECO:0000256|SAAS:SAAS00356446};
DE            EC=1.7.1.13 {ECO:0000256|HAMAP-Rule:MF_00818, ECO:0000256|SAAS:SAAS00356477};
DE   AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000256|HAMAP-Rule:MF_00818};
DE   AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00818};
DE   AltName: Full=PreQ(0) reductase {ECO:0000256|HAMAP-Rule:MF_00818};
GN   Name=queF {ECO:0000256|HAMAP-Rule:MF_00818};
GN   OrderedLocusNames=Bsel_0027 {ECO:0000313|EMBL:ADH97578.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97578.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97578.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7-
CC       deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
CC       {ECO:0000256|HAMAP-Rule:MF_00818, ECO:0000256|SAAS:SAAS00356452}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-
CC         deazaguanine + 3 H(+) + 2 NADPH; Xref=Rhea:RHEA:13409,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:45075, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58703; EC=1.7.1.13;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00818,
CC         ECO:0000256|SAAS:SAAS01120123};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00818, ECO:0000256|SAAS:SAAS00184003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00818,
CC       ECO:0000256|SAAS:SAAS00356463}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type
CC       1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00818,
CC       ECO:0000256|SAAS:SAAS00549179}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00818}.
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DR   EMBL; CP001791; ADH97578.1; -; Genomic_DNA.
DR   RefSeq; WP_013171008.1; NC_014219.1.
DR   STRING; 439292.Bsel_0027; -.
DR   EnsemblBacteria; ADH97578; ADH97578; Bsel_0027.
DR   KEGG; bse:Bsel_0027; -.
DR   eggNOG; ENOG4105CSD; Bacteria.
DR   eggNOG; COG0780; LUCA.
DR   HOGENOM; HOG000009527; -.
DR   KO; K09457; -.
DR   OMA; CPITSQP; -.
DR   OrthoDB; 1675155at2; -.
DR   BioCyc; BSEL439292:G1GLR-34-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046857; F:oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0033739; F:preQ1 synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00818; QueF_type1; 1.
DR   InterPro; IPR029500; QueF.
DR   InterPro; IPR016856; QueF_type1.
DR   Pfam; PF14489; QueF; 1.
DR   TIGRFAMs; TIGR03139; QueF-II; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XV20.
DR   SWISS-2DPAGE; D6XV20.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00818,
KW   ECO:0000256|SAAS:SAAS00184021};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00818, ECO:0000256|SAAS:SAAS00434347};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00818,
KW   ECO:0000256|SAAS:SAAS00184022};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00818,
KW   ECO:0000256|SAAS:SAAS00184005};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   REGION       72     74       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00818}.
FT   ACT_SITE     50     50       Thioimide intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00818}.
FT   ACT_SITE     57     57       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00818}.
SQ   SEQUENCE   135 AA;  15193 MW;  9DD69F5972E9785E CRC64;
     MSENYYLPRS GPMPRPASVE EGRNVLRDEA FPAPDVSVVR FKALEFTAVC PKTGQPDFGQ
     VEIEYVPRNK CIESKSLKFY LWSYRDEGAY CESLAAQIAD DVMAAIEPAR VKVMVHQTPR
     GGIQLETEAE RIHEA
//

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