(data stored in SCRATCH zone)

SWISSPROT: B4SSM9_STRM5

ID   B4SSM9_STRM5            Unreviewed;       803 AA.
AC   B4SSM9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN   OrderedLocusNames=Smal_0206 {ECO:0000313|EMBL:ACF49911.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49911.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49911.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49911.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC         diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC         diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698,
CC         Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316;
CC         EC=1.17.4.1; Evidence={ECO:0000256|RuleBase:RU003410};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|RuleBase:RU003410}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
CC       large chain family. {ECO:0000256|RuleBase:RU003410}.
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DR   EMBL; CP001111; ACF49911.1; -; Genomic_DNA.
DR   RefSeq; WP_004136104.1; NC_011071.1.
DR   STRING; 391008.Smal_0206; -.
DR   EnsemblBacteria; ACF49911; ACF49911; Smal_0206.
DR   KEGG; smt:Smal_0206; -.
DR   eggNOG; ENOG4105BZH; Bacteria.
DR   eggNOG; COG0209; LUCA.
DR   HOGENOM; HOG000057035; -.
DR   KO; K00525; -.
DR   OMA; CSEIMLP; -.
DR   OrthoDB; 357568at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01040-MONOMER; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR013346; NrdE_NrdA.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   PANTHER; PTHR11573; PTHR11573; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   SUPFAM; SSF48168; SSF48168; 1.
DR   TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SSM9.
DR   SWISS-2DPAGE; B4SSM9.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00492,
KW   ECO:0000256|SAAS:SAAS00460659};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   DNA replication {ECO:0000256|RuleBase:RU003410};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00492,
KW   ECO:0000256|SAAS:SAAS00460691};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003410,
KW   ECO:0000313|EMBL:ACF49911.1}.
FT   DOMAIN       26    115       ATP-cone. {ECO:0000259|PROSITE:PS51161}.
SQ   SEQUENCE   803 AA;  89673 MW;  F9F539413E0AEE77 CRC64;
     MTTESSATIE KESEFLLTSP PTANAMSVTK RNGTTELVDL NKIVRAVQRS SEGLHAVDPM
     RVATRTISGL YNGATTRELD ELSIRTAALL IGEEPEYGRL AARLLANYIA KEVSGQEIYA
     FSQSVGRGHE VGLINDRLLN FVQTNARKLN DAIDMSLDLN FDYFGLRTLY DRYLLRHPHT
     RKVIETPQQF FLRIASALSE DVPEALALYK RMGNLDYLPS SPTLFNSGTT HEQLSSCFLL
     DSPQDSLESI YSKYGDIAQL SKFSGGIGVS YTRVRSRGSL IKSTNGHSNG IVPWLKTMDS
     SVAAVNQGGK RKGAACVYLE TWHADVEDFL ELRDNTGDES RRAHNLNLAN WIPDLFMKRV
     EADQEWSLFD PRVVPEFTDL FGEAFEAAYL QAEAQGKANR TISARKLYSR MMRTLAETGN
     GWMTFKDKCN RASNQTLRAG NVIHLSNLCT EILEVTSAEE TAVCNLGSIN LGNHFDGNGE
     FDFDKLADTV RLAVRQLDRV IDLNFYPIES ARRGNLRWRP VGLGCMGLQD VFFRKRLPFD
     GAEARALSKK IAETIYFHAL ETSVELAQER GKHPSFADTR AASGELQFDA WNVVPEDAER
     WDSLRERIKE HGLRNSLMIA IAPTATIASI AGCYECVEPQ VSNLFKRETL SGDFLQVNRY
     LVNELKKLGH WTPEMRDAIK LAEGSIQGIT QIPETLRHVY RTAWELPMRS LIDMAADRGA
     FIDQSASLNL FMESPNIGAM SSMYMYAWKQ GIKTTYYLRS RPATKIAKTT VSHAAGAAPE
     KVFSPEEAIA CSLENPEACE ACQ
//

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