(data stored in ACNUC1104 zone)

SWISSPROT: D3UWE8_XENBS

ID   D3UWE8_XENBS            Unreviewed;       281 AA.
AC   D3UWE8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000256|HAMAP-Rule:MF_00817, ECO:0000256|SAAS:SAAS00337114};
DE            EC=1.7.1.13 {ECO:0000256|HAMAP-Rule:MF_00817, ECO:0000256|SAAS:SAAS00356735};
DE   AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000256|HAMAP-Rule:MF_00817};
DE   AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00817};
DE   AltName: Full=PreQ(0) reductase {ECO:0000256|HAMAP-Rule:MF_00817};
GN   Name=queF {ECO:0000256|HAMAP-Rule:MF_00817};
GN   OrderedLocusNames=XBJ1_0578 {ECO:0000313|EMBL:CBJ79722.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79722.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79722.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79722.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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_00817, ECO:0000256|SAAS:SAAS00337124}.
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_00817,
CC         ECO:0000256|SAAS:SAAS01117020};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00817, ECO:0000256|SAAS:SAAS00037299}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00817,
CC       ECO:0000256|SAAS:SAAS00337134}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00817,
CC       ECO:0000256|SAAS:SAAS00356791}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type
CC       2 subfamily. {ECO:0000256|HAMAP-Rule:MF_00817,
CC       ECO:0000256|SAAS:SAAS00534868}.
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DR   EMBL; FN667741; CBJ79722.1; -; Genomic_DNA.
DR   RefSeq; WP_012987176.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0578; -.
DR   EnsemblBacteria; CBJ79722; CBJ79722; XBJ1_0578.
DR   GeneID; 8830200; -.
DR   KEGG; xbo:XBJ1_0578; -.
DR   PATRIC; fig|406818.4.peg.532; -.
DR   eggNOG; ENOG4107R1K; Bacteria.
DR   eggNOG; COG0780; LUCA.
DR   eggNOG; COG2904; LUCA.
DR   HOGENOM; HOG000273755; -.
DR   KO; K06879; -.
DR   OMA; QCVERIY; -.
DR   BioCyc; XBOV406818:XBJ1_RS02510-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000002045; 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_00817; QueF_type2; 1.
DR   InterPro; IPR029500; QueF.
DR   InterPro; IPR029139; QueF_N.
DR   InterPro; IPR016428; QueF_type2.
DR   Pfam; PF14489; QueF; 1.
DR   Pfam; PF14819; QueF_N; 1.
DR   PIRSF; PIRSF004750; Nitrile_oxidored_YqcD_prd; 1.
DR   TIGRFAMs; TIGR03138; QueF; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UWE8.
DR   SWISS-2DPAGE; D3UWE8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00817,
KW   ECO:0000256|SAAS:SAAS00434468};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00817, ECO:0000256|SAAS:SAAS00434499};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00817,
KW   ECO:0000256|SAAS:SAAS00434467};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00817,
KW   ECO:0000256|SAAS:SAAS00434474};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN       21    130       QueF_N. {ECO:0000259|Pfam:PF14819}.
FT   NP_BIND      90     91       NADPH. {ECO:0000256|HAMAP-Rule:MF_00817}.
FT   NP_BIND     257    258       NADPH. {ECO:0000256|HAMAP-Rule:MF_00817}.
FT   REGION       88     90       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00817}.
FT   REGION      228    229       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00817}.
FT   ACT_SITE    189    189       Thioimide intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00817}.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00817}.
SQ   SEQUENCE   281 AA;  32158 MW;  67F31FDF6D55B688 CRC64;
     MSLYQDNQAL AQLTLGKPTP YRDHYDPTLL QAVPRSMNRE PLGLFPDNLP FHGADIWTLY
     ELSWLNTRGV PQVAIGHVSL NAASVSLIES KSFKLYLNSF NQTRFADWDT VQKTLQQDLS
     VCANGEVNVV LHPLHDFSQQ PIAEFEGKCI DNQDIEIDDY QFSRDYLNGA ATGSVVDEIL
     VSHLLKSNCL ITHQPDWGSV QIRYKGPKID QEKLLRYLVS FRHHNEFHEQ CVERIFNDLI
     ALCAPEKLTV YARYTRRGGL DINPWRSNEA FIPETGRLAR Q
//

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