(data stored in ACNUC7421 zone)

SWISSPROT: D4YYU4_SPHJU

ID   D4YYU4_SPHJU            Unreviewed;       157 AA.
AC   D4YYU4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000256|HAMAP-Rule:MF_00818, ECO:0000256|SAAS:SAAS00337115};
DE            EC=1.7.1.13 {ECO:0000256|HAMAP-Rule:MF_00818, ECO:0000256|SAAS:SAAS00337103};
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=ykvM {ECO:0000313|EMBL:BAI95526.1};
GN   Synonyms=queF {ECO:0000256|HAMAP-Rule:MF_00818,
GN   ECO:0000313|EMBL:BAI95526.1};
GN   OrderedLocusNames=SJA_C1-06920 {ECO:0000313|EMBL:BAI95526.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95526.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95526.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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:SAAS00534865}.
CC   -!- CATALYTIC ACTIVITY: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-
CC       cyano-7-carbaguanine + 2 NADPH. {ECO:0000256|HAMAP-Rule:MF_00818,
CC       ECO:0000256|SAAS:SAAS00337109}.
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00818, ECO:0000256|SAAS:SAAS00337123}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00818,
CC       ECO:0000256|SAAS:SAAS00337135}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type
CC       1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00818,
CC       ECO:0000256|SAAS:SAAS00534867}.
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DR   EMBL; AP010803; BAI95526.1; -; Genomic_DNA.
DR   STRING; 452662.SJA_C1-06920; -.
DR   EnsemblBacteria; BAI95526; BAI95526; SJA_C1-06920.
DR   KEGG; sjp:SJA_C1-06920; -.
DR   eggNOG; ENOG4105CSD; Bacteria.
DR   eggNOG; COG0780; LUCA.
DR   HOGENOM; HOG000009527; -.
DR   KO; K09457; -.
DR   OMA; CPITSQP; -.
DR   OrthoDB; POG091H01A3; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000007753; Chromosome 1.
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-HAMAP.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00818; QueF_type1; 1.
DR   InterPro; IPR029500; QueF.
DR   InterPro; IPR016856; QueF_type1.
DR   Pfam; PF14489; QueF; 1.
DR   PIRSF; PIRSF027377; Nitrile_oxidored_QueF; 1.
DR   TIGRFAMs; TIGR03139; QueF-II; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYU4.
DR   SWISS-2DPAGE; D4YYU4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00818,
KW   ECO:0000256|SAAS:SAAS00001344};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00818, ECO:0000256|SAAS:SAAS00415727};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00818,
KW   ECO:0000256|SAAS:SAAS00415714, ECO:0000313|EMBL:BAI95526.1};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00818,
KW   ECO:0000256|SAAS:SAAS00001353};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   REGION       77     79       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00818}.
FT   REGION       96     97       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00818}.
FT   ACT_SITE     55     55       Thioimide intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00818}.
FT   ACT_SITE     62     62       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00818}.
SQ   SEQUENCE   157 AA;  17295 MW;  E873F65E9FE92AC1 CRC64;
     MTDMPTPLQP SPIHLGQTSA LPARPEDAVL DYVPNPRPGK PYLVRFTAPE FTSLCPVTGQ
     PDFAHLVIDY APAATIVESK SLKLFLGAFR NHAAFHEDCT VGIGERLFAE MNPIWLRIGG
     YWYPRGGIPI DVFWQSGEPP AGLWLPPQDV PGYRGRG
//

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