ID B0N686_9FIRM Unreviewed; 846 AA.
AC B0N686;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=CLORAM_02107 {ECO:0000313|EMBL:EDS17324.1};
OS Thomasclavelia ramosa DSM 1402.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=445974 {ECO:0000313|EMBL:EDS17324.1, ECO:0000313|Proteomes:UP000005798};
RN [1] {ECO:0000313|EMBL:EDS17324.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS17324.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium ramosum(DSM 1402).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS17324.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS17324.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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:EDS17324.1}.
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DR EMBL; ABFX02000008; EDS17324.1; -; Genomic_DNA.
DR AlphaFoldDB; B0N686; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_9; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000005798; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR005144; ATP-cone_dom.
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; PF03477; ATP-cone; 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; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000005798}.
FT DOMAIN 12..100
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 846 AA; 97854 MW; B7805F13770E826E CRC64;
MLEWHSKDVK KMLIQKRNGL FQDYDNNKIE TAIKKAFCSL SETIKDDELK KMIADIEKHI
IADMSVEAIQ DLVEETLMKH GYLQVAKAYI LYRQKHTEQR LIIDELLALL GDQNLKKVLL
KIHKDYPQEE YSLQLLLVKF KTFYKEGMSH FEALKMLMKA SVELISKEAP KWEMISARFL
TYDVNQQVDQ KMNTAGRYTF YERINYLAQQ GYYGQYILES YSKDEIDMLG QYISESRNEL
FTYSGLELIV KRYLIQNHDR EIIEKPQEMF MSIAMHLAMN ESNRVKWAKE IYDILSTLKV
TMATPTMSNA RKPFHQMSSC FIDTVDDSLA GIYKSIDNFA KVSKNGGGMG LYFGKVRANG
SSIRGFKGAA GGVIRWLKLV NDTATAVDQL GVRQGAAAVY LDAWHKDLPE FLQIRTNNGD
DRMKAHDIFP AVCYPDLFWK LAKNDLEASW YMMCPHEIHE VKGYYLEDCY GEEWERKYYE
CVEDDRIPKR VMTVKEIVRL IIKSLVETGT PFTFNRDHVN NFNPNPHQGM IYCSNLCTEI
AQNMQAMEIL PSEEIEVNGE TIIVEKTKPG DFVVCNLASL TLGHLDVLND DELRHVISVV
IRALDNVIDL NYYPIPFAKI TNQKYRAIGL GTSGYHHMLV KLKMSFESDE HLQFIEQLYE
KINYFALEAS CDLAKEKGSY SLFNGSDFET GAYFIKRRYQ SKAWQNLQAK IKENGLRNGY
LLAIAPTSST SIIAGTTAAV DPIMKKYFME EKKGSMITRV APDLDSETFW LYKNAHYIDQ
EWIVKAAGIR QRHLDQSQSV NLYMTNEFTF RKLLNLYIKA WEYGVKTLYY VRSQSLEVEE
CESCSS
//
