ID F8G781_FRAST Unreviewed; 590 AA.
AC F8G781;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=F7308_1264 {ECO:0000313|EMBL:AEI36190.1};
OS Francisella salina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=573569 {ECO:0000313|EMBL:AEI36190.1, ECO:0000313|Proteomes:UP000000490};
RN [1] {ECO:0000313|Proteomes:UP000000490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX07-7308 {ECO:0000313|Proteomes:UP000000490};
RA Kuske C.R., Challacombe J.F., Siddaramappa S., Petersen J.M.;
RT "The complete genome of Francisella sp. TX077308.";
RL Submitted (MAY-2011) 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, 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; CP002872; AEI36190.1; -; Genomic_DNA.
DR RefSeq; WP_013923024.1; NC_015696.1.
DR AlphaFoldDB; F8G781; -.
DR STRING; 573569.F7308_1264; -.
DR KEGG; frt:F7308_1264; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_7_0_6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000490; 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; 1.
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}.
FT DOMAIN 18..83
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 93..402
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 590 AA; 66294 MW; C417153DB0FC4A93 CRC64;
MSNEKYLGIH IDISKDHELS EQAQQLLTNY YCLENEPSPQ YAFARASVAY SFGDMNLAQR
IYDAASKGWF MFASPVLSNA PLPGAKVKSL PISCFLSYVP DSLEGLIEHS SELRWLSVKG
GGVGGHWSNV RAVSDKAPGP IPFMHTVDAD MVAYRQGKTR KGSYAAYMDV SHPDIVEFLG
IRVPTGDVNR KCLNLHHAVN LTDDFMQAVA DDADWKLVDP DDKTVRDIVK ARKIWETILE
TRYRTGEPYL NFIDTANRAL PKSQKELGLT IKGSNLCNEI HLVTDEKRTA VCCLSSVNLE
KYDEWKGTSL IKDLIRFLDN VLQFFIDHAG DEISKARYSA SRERSLGLGA MGFHSYLQKH
NVPFESQKAK EINEEIFKRI KEQAVEETLI LGSEKGEAPD MAGTGRRNAH LLAIAPNANS
SLILNTSPSI EPWKANAFTS RTRVGSHLTK NKYLERELEK VGKNTEEVWS DIITNGGSVQ
QLEFLSDDIK AVFKTAIEMD QDWVVYLGGQ RQNHLCQGQS LNIFFPAGAS RGYLHKVHFN
AWKYGCKGLY YLRTETSNRA ENISKKVEKN RLVEFSELKQ SENECIACEG
//
