ID   A0A0K0GB06_9FIRM        Unreviewed;       745 AA.
AC   A0A0K0GB06;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
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   ORFNames=WH51_08205 {ECO:0000313|EMBL:KKE79250.1};
OS   Bacilli bacterium VT-13-104.
OC   Bacteria; Bacillota; Bacilli.
OX   NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE79250.1, ECO:0000313|Proteomes:UP000034981};
RN   [1] {ECO:0000313|Proteomes:UP000034981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VT-13-104 {ECO:0000313|Proteomes:UP000034981};
RA   Tetz V., Tetz G.;
RT   "Bacilli bacterium VT-13-104.";
RL   Submitted (APR-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKE79250.1}.
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DR   EMBL; LAZH01000033; KKE79250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K0GB06; -.
DR   PATRIC; fig|1637974.4.peg.1721; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000034981; Unassembled WGS sequence.
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; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
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.
DR   PROSITE; PS00089; RIBORED_LARGE; 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:UP000034981}.
FT   DOMAIN          602..624
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   745 AA;  85942 MW;  ACEF4AD2FD027167 CRC64;
     MIGEMVKESE KLNKVIEKAA KGLSLDIGLF IEKVETSLNH YQEYEKGLDF LIKKALEEID
     EANPDWSFFA ARLYLQRLYK QAAINRNYDD KNKKYGSFLK LIKSLTDKGI YSSHFLGKYT
     EDEINYFGDL IDPDKDMNFT YLGIYTLATR YLATDFEKNT HELPQERWMI IAMHLMQNED
     KSRRTQLVEE AYWALSNLYM TVATPTLANA GKTHGQLSSC FIDTVDDSLQ SIYDSNTDIA
     RLSKNGGGIG VYMGKIRSRG SDIKGFKGMS SGVIPWIKQL NNTAVSVDQL GTRKGAIAVY
     LDVWHRDIEA FLDLKLNNGD DRMRAHDIFT GVCLPDYFME QVDKRGEWYL FDPHEIRQVM
     GFSLEDYFDE QKGSGSFREK YEQCIEAPLQ SKRKVPAIDI MKRIMRSQLE SGTPFMFYRD
     EVNRKNSNAH TGIIYCSNLC TEITQNQSPS EFLEEYVENE ETIVKKYKPG DYVVCNLSSI
     NLGKAVPEGV LERLIPIQVR MLDNVIDINT LPIKQAERTN KKYRAIGLGT FGWHHLLAVM
     GIKWETEEAV QYADTLYEKI AYLTIKSSMK LSKEKGHYPE FHGSKWSTGA YFEEKGYKDD
     TWIKLMEEVK ENGMRNAYLM AVAPNSTTAM IAGSTASIDP IFKPFYYEEK KDFKIPVTAP
     DIDHRTYDIY RRSAYIVDQR WSIKQNAARQ KHIDQSISFN FYVPNTIRAS VLLDLHLQAW
     REGLKTTYYV RSTSNDVEEC EWCQS
//