ID   NRDD_ECOLI              Reviewed;         712 AA.
AC   P28903; Q2M669;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   25-NOV-2008, entry version 75.
DE   RecName: Full=Anaerobic ribonucleoside-triphosphate reductase;
DE            EC=1.17.4.2;
GN   Name=nrdD; OrderedLocusNames=b4238, JW4197;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=93133831; PubMed=8421692;
RA   Sun X., Harder J., Krook M., Joernvall H., Sjoeberg B.-M.,
RA   Reichard P.;
RT   "A possible glycine radical in anaerobic ribonucleotide reductase from
RT   Escherichia coli: nucleotide sequence of the cloned nrdD gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:577-581(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=95334362; PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
RA   Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT   region from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-229.
RC   STRAIN=K12;
RX   MEDLINE=94364944; PubMed=8083158;
RA   Rimmele M., Boos W.;
RT   "Trehalose-6-phosphate hydrolase of Escherichia coli.";
RL   J. Bacteriol. 176:5654-5664(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 703-712.
RC   STRAIN=K12;
RX   MEDLINE=95155298; PubMed=7852304; DOI=10.1074/jbc.270.6.2443;
RA   Sun X., Eliasson R., Pontis E., Andersson J., Buist G.,
RA   Sjoeberg B.-M., Reichard P.;
RT   "Generation of the glycyl radical of the anaerobic Escherichia coli
RT   ribonucleotide reductase requires a specific activating enzyme.";
RL   J. Biol. Chem. 270:2443-2446(1995).
RN   [7]
RP   MUTAGENESIS OF CYSTEINE RESIDUES, AND ENZYME ACTIVITY.
RX   PubMed=12655046; DOI=10.1073/pnas.0736456100;
RA   Logan D.T., Mulliez E., Larsson K.-M., Bodevin S., Atta M.,
RA   Garnaud P.E., Sjoeberg B.-M., Fontecave M.;
RT   "A metal-binding site in the catalytic subunit of anaerobic
RT   ribonucleotide reductase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:3826-3831(2003).
CC   -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside triphosphate +
CC       thioredoxin disulfide + H(2)O = ribonucleoside triphosphate +
CC       thioredoxin.
CC   -!- SUBUNIT: Tetramer consisting of 2 alpha (NrdD) and 2 beta (NrdG)
CC       subunits.
CC   -!- INTERACTION:
CC       P18843:nadE; NbExp=1; IntAct=EBI-370011, EBI-548960;
CC   -!- INDUCTION: Probably by nrdD-activating enzyme under anaerobic
CC       conditions by generation of an organic free radical. Exposure of
CC       activated nrdD to oxygen may result in cleavage at the glycine
CC       residue harboring its organic radical with loss of the 31 C-
CC       terminal AA.
CC   -!- SIMILARITY: Belongs to the anaerobic ribonucleoside-triphosphate
CC       reductase family.
CC   -!- SIMILARITY: Contains 1 ATP-cone domain.
CC   -!- SIMILARITY: Contains 1 glycine radical domain.
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DR   EMBL; L06097; AAA24226.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97135.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77195.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78237.1; -; Genomic_DNA.
DR   EMBL; U06195; AAC43383.1; -; Genomic_DNA.
DR   EMBL; Z46865; CAA86938.1; -; Genomic_DNA.
DR   PIR; A47331; A47331.
DR   RefSeq; AP_004736.1; -.
DR   RefSeq; NP_418659.1; -.
DR   HSSP; P07071; 1H78.
DR   IntAct; P28903; -.
DR   GeneID; 948755; -.
DR   GenomeReviews; U00096_GR; b4238.
DR   GenomeReviews; AP009048_GR; JW4197.
DR   KEGG; ecj:JW4197; -.
DR   KEGG; eco:b4238; -.
DR   EchoBASE; EB1388; -.
DR   EcoGene; EG11417; nrdD.
DR   HOGENOM; P28903; -.
DR   BioCyc; EcoCyc:RIBONUCLEOSIDE-TRIP-REDUCT-MON; -.
DR   BioCyc; MetaCyc:RIBONUCLEOSIDE-TRIP-REDUCT-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR005144; ATP-cone.
DR   InterPro; IPR001150; Form_AcTrfase_GR.
DR   InterPro; IPR012833; NrdD.
DR   Pfam; PF03477; ATP-cone; 1.
DR   Pfam; PF01228; Gly_radical; 1.
DR   TIGRFAMs; TIGR02487; NrdD; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
DR   PROSITE; PS00850; GLY_RADICAL_1; 1.
DR   PROSITE; PS51149; GLY_RADICAL_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Direct protein sequencing;
KW   Metal-binding; Nucleotide-binding; Organic radical; Oxidoreductase;
KW   Zinc.
FT   CHAIN         1    712       Anaerobic ribonucleoside-triphosphate
FT                                reductase.
FT                                /FTId=PRO_0000166683.
FT   DOMAIN        3     92       ATP-cone.
FT   DOMAIN      583    708       Glycine radical.
FT   METAL       644    644       Zinc.
FT   METAL       647    647       Zinc.
FT   METAL       662    662       Zinc.
FT   METAL       665    665       Zinc.
FT   MOD_RES     681    681       Glycine radical (By similarity).
FT   CONFLICT    257    257       G -> R (in Ref. 1; AAA24226).
FT   CONFLICT    420    420       A -> P (in Ref. 1; AAA24226).
SQ   SEQUENCE   712 AA;  80023 MW;  943589D653EB0C38 CRC64;
     MTPHVMKRDG CKVPFKSERI KEAILRAAKA AEVDDADYCA TVAAVVSEQM QGRNQVDINE
     IQTAVENQLM SGPYKQLARA YIEYRHDRDI EREKRGRLNQ EIRGLVEQTN ASLLNENANK
     DSKVIPTQRD LLAGIVAKHY ARQHLLPRDV VQAHERGDIH YHDLDYSPFF PMFNCMLIDL
     KGMLTQGFKM GNAEIEPPKS ISTATAVTAQ IIAQVASHIY GGTTINRIDE VLAPFVTASY
     NKHRKTAEEW NIPDAEGYAN SRTIKECYDA FQSLEYEVNT LHTANGQTPF VTFGFGLGTS
     WESRLIQESI LRNRIAGLGK NRKTAVFPKL VFAIRDGLNH KKGDPNYDIK QLALECASKR
     MYPDILNYDQ VVKVTGSFKT PMGCRSFLGV WENENGEQIH DGRNNLGVIS LNLPRIALEA
     KGDEATFWKL LDERLVLARK ALMTRIARLE GVKARVAPIL YMEGACGVRL NADDDVSEIF
     KNGRASISLG YIGIHETINA LFGGEHVYDN EQLRAKGIAI VERLRQAVDQ WKEETGYGFS
     LYSTPSENLC DRFCRLDTAE FGVVPGVTDK GYYTNSFHLD VEKKVNPYDK IDFEAPYPPL
     ANGGFICYGE YPNIQHNLKA LEDVWDYSYQ HVPYYGTNTP IDECYECGFT GEFECTSKGF
     TCPKCGNHDA SRVSVTRRVC GYLGSPDARP FNAGKQEEVK RRVKHLGNGQ IG
//