ID N9WMP9_CLOIN Unreviewed; 838 AA.
AC N9WMP9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=HMPREF1094_03708 {ECO:0000313|EMBL:ENY84711.1};
OS [Clostridium] innocuum 2959.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=999413 {ECO:0000313|EMBL:ENY84711.1, ECO:0000313|Proteomes:UP000013051};
RN [1] {ECO:0000313|EMBL:ENY84711.1, ECO:0000313|Proteomes:UP000013051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2959 {ECO:0000313|EMBL:ENY84711.1,
RC ECO:0000313|Proteomes:UP000013051};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium innocuum 2959.";
RL Submitted (JAN-2013) 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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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:ENY84711.1}.
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DR EMBL; AGYV01000007; ENY84711.1; -; Genomic_DNA.
DR RefSeq; WP_002609534.1; NZ_KB850945.1.
DR AlphaFoldDB; N9WMP9; -.
DR GeneID; 61927125; -.
DR PATRIC; fig|999413.4.peg.3965; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_9; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000013051; 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:UniProtKB-UniPathway.
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:UP000013051}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 838 AA; 96844 MW; 51C2D4B90D44C454 CRC64;
MKIQKRDGQL QEFEGEKIAQ AIRKAFRSTG TLIEEAVLKE IIEDITKAAA ADKPMLSVEV
VQDLVEEELM QHQFYKEAKN YILYRQKRTE SRKVVQDLVH ALQKEDLYSI LADIQQRYPD
EGYDLRHLLM KFHSFLKEDM ESDERLHMLM KASVELISKE APKWEYIASR FLSYALHEEI
SARMQKLELP VFSKKLKYLE EQGYYGDYIR KAYSDAEIDE LGAYLKDERD YLFTYSGLEL
VKKRYLMCSH AHEVLETPQE MFMGIAMHLA LPEQNRMYWA KQIYDILSQL QVTMATPTMS
NARKPYHQLS SCFIDTVEDT LNNIYKSVDN FAQVSKYGGG MGLYFGKVRA NGSDIRGFEG
AAGGVIRWIK LVNDTATAVD QLGVRQGAVA VYLDAWHKDL PEFLNLRTNN GDDRMKAHDV
FPAVCYPDLF WKMAKEDLNA TWYLMCPHEI HKIKGYHLED FYGEEWEERY FDCVQDPRVP
KRTMVLKDLV RLILKSAVET GTPFTFNRDH VNRMNPNAHA GMIYCSNLCT EIAQNMKALK
LEESRIVEID GESVVVNESK PGDFVVCNLA SLSLGNIDVN NEEELSHIIH VIVRALDNVI
DLNYYPIPYA KITNRKYRPI GLGVSGYHHM LVKQNLRFES EEHLQYADTL FEKINYYAIQ
ASTALAREKG SYSMFAGSDW QSGAYFTKRG YTSDAWSRLF RQVREQGMRN AWLMAIAPTS
STSIIAGTTA GVDPIMNKYY LEEKKGSMIA RVAPDLDART FWLYKNAHLI DQEWVVRSAG
IRQRHIDQAQ SVNLYITNEF TLRQVLMLYI HAWEYGVKTI YYVRSKSLEV EECESCAS
//