ID Q9ZD34_RICPR Unreviewed; 607 AA.
AC Q9ZD34;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN OrderedLocusNames=RP513 {ECO:0000313|EMBL:CAA14965.1};
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947 {ECO:0000313|EMBL:CAA14965.1, ECO:0000313|Proteomes:UP000002480};
RN [1] {ECO:0000313|EMBL:CAA14965.1, ECO:0000313|Proteomes:UP000002480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E {ECO:0000313|EMBL:CAA14965.1,
RC ECO:0000313|Proteomes:UP000002480};
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; AJ235272; CAA14965.1; -; Genomic_DNA.
DR PIR; C71655; C71655.
DR RefSeq; NP_220889.1; NC_000963.1.
DR RefSeq; WP_004599079.1; NC_000963.1.
DR AlphaFoldDB; Q9ZD34; -.
DR SMR; Q9ZD34; -.
DR STRING; 272947.gene:17555593; -.
DR EnsemblBacteria; CAA14965; CAA14965; CAA14965.
DR GeneID; 57569635; -.
DR KEGG; rpr:RP513; -.
DR PATRIC; fig|272947.5.peg.523; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_7_0_5; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
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; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000002480}.
FT DOMAIN 21..85
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 89..409
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 418..563
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 607 AA; 68733 MW; B438BFB3C066B553 CRC64;
MNTLKKNKFQ ITINNKYNNL LTPFGKAILR DRYLMKGEDF QDLFARVSSH YAENKQHAQK
LYEYMSQMWF MPATPILSNG GTERGLPISC FLNETDDSLD DIVNLWMENV WLAARGGGIG
SYWGNVRSIN EAIRDKGHSS GIIPFIKVMD SMTLAISQGS IRRGSSAVYL PINHPEIEEF
IDIRRPTGGD VNRKSLNIHH GITITDEFMQ AVENNMDFDL VSPATKKVAN KVRARDLWIK
LLTTRIETGE PYLLFIDSVN KTIPEHHKKL GLQVKMSNLC SEITLPTGID HLGNSRTAVC
CLASLNLEYY EVWKDDKEFI HSIMLFLDNV LEDFINKAPN TMARAKYAAF RERSVGLGVI
GFHSFLQMKK IPIESVMAKV WNKKIFEYIS AEVDKASIEI GKDKGACPDA LDSGSNERFS
NKTAIAPTAS ISVIAGNASP GIEPFAANSF VQKTLTGSFN VRNKHLEQLL EEKGFNNDQV
WSSIATHEGS VQHLTFLSEE EKQIFKTAYE IDQNWLIELA ADRTPYITQS QALNIFLHGN
VSKKYLNNIH FKAWKKGIKS LYYCRSTSIQ RADKVSHDVL KADFKDLEKQ NDKLAQTRNY
EECLACQ
//
