(data stored in SCRATCH zone)

SWISSPROT: B4SSN0_STRM5

ID   B4SSN0_STRM5            Unreviewed;       339 AA.
AC   B4SSN0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355};
DE            EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355};
GN   OrderedLocusNames=Smal_0207 {ECO:0000313|EMBL:ACF49912.1};
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:ACF49912.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49912.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49912.1,
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|PIRNR:PIRNR000355}.
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|PIRNR:PIRNR000355};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000355,
CC         ECO:0000256|PIRSR:PIRSR000355-2};
CC       Note=Binds 2 iron ions per subunit.
CC       {ECO:0000256|PIRNR:PIRNR000355, ECO:0000256|PIRSR:PIRSR000355-2};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|PIRNR:PIRNR000355}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
CC       small chain family. {ECO:0000256|PIRNR:PIRNR000355}.
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DR   EMBL; CP001111; ACF49912.1; -; Genomic_DNA.
DR   RefSeq; WP_012509755.1; NC_011071.1.
DR   STRING; 391008.Smal_0207; -.
DR   EnsemblBacteria; ACF49912; ACF49912; Smal_0207.
DR   KEGG; smt:Smal_0207; -.
DR   eggNOG; ENOG4105E05; Bacteria.
DR   eggNOG; COG0208; LUCA.
DR   HOGENOM; HOG000255975; -.
DR   KO; K00526; -.
DR   OMA; HWESLKP; -.
DR   OrthoDB; 1384440at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01045-MONOMER; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; -; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; PTHR23409; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   PIRSF; PIRSF000355; NrdB; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SSN0.
DR   SWISS-2DPAGE; B4SSN0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   DNA replication {ECO:0000256|PIRNR:PIRNR000355};
KW   Iron {ECO:0000256|PIRNR:PIRNR000355, ECO:0000256|PIRSR:PIRSR000355-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000355,
KW   ECO:0000256|PIRSR:PIRSR000355-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000355,
KW   ECO:0000313|EMBL:ACF49912.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    169    194       Helical. {ECO:0000256|SAM:Phobius}.
FT   ACT_SITE    113    113       {ECO:0000256|PIRSR:PIRSR000355-1}.
FT   METAL        75     75       Iron 1. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       106    106       Iron 1. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       106    106       Iron 2. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       109    109       Iron 1. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       181    181       Iron 2. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       215    215       Iron 2. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       218    218       Iron 2. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
SQ   SEQUENCE   339 AA;  39786 MW;  35A43568480C83BF CRC64;
     MADKPKQMLL DPGFELTLRP MRYPQFYDMY RNAIKNTWTV EEINFQIDIS DLHSKMSPGE
     RHLIHRLVAF FATGDSIVSN NLVLNLYQHL NAPEARMYLS RQLYEEALHV QFYLTLLDNY
     LPDPDERVKA FAAVENIDSI KKKADFCFKW IDSIQNLKRI ETREERRQFL LNQICFAACI
     EGLFFFAAFA YVYYFRSRGL LNGLASGTNW VFRDESAHMD FAFECVDVIR EEEPDLFDDK
     MKQDVYDMLA EAIECEVQFA EDVLSGGVAG ISTRDMRQYL QHCADNHFHR LGMERKYNVR
     NPLSFMELQD VQELTNFFER RASAYQVGVQ GEVAFDMNF
//

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