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Entry: N9WMP9_CLOIN
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Original site: N9WMP9_CLOIN 
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
//
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