ID K0YMC3_9ACTN Unreviewed; 851 AA.
AC K0YMC3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=HMPREF9451_00179 {ECO:0000313|EMBL:EJZ84576.1};
OS Slackia piriformis YIT 12062.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Slackia.
OX NCBI_TaxID=742818 {ECO:0000313|EMBL:EJZ84576.1, ECO:0000313|Proteomes:UP000006069};
RN [1] {ECO:0000313|EMBL:EJZ84576.1, ECO:0000313|Proteomes:UP000006069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12062 {ECO:0000313|EMBL:EJZ84576.1,
RC ECO:0000313|Proteomes:UP000006069};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Slackia piriformis YIT 12062.";
RL Submitted (AUG-2012) 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:EJZ84576.1}.
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DR EMBL; ADMD01000001; EJZ84576.1; -; Genomic_DNA.
DR RefSeq; WP_009138416.1; NZ_JH815198.1.
DR AlphaFoldDB; K0YMC3; -.
DR PATRIC; fig|742818.3.peg.202; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_11; -.
DR InParanoid; K0YMC3; -.
DR OrthoDB; 9804622at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000006069; 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:UP000006069}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 851 AA; 95978 MW; A06493BBD3A3C0EB CRC64;
MDIVKRSGAT EAYDGSKIVA AIAGAFSDVN REASEETLAA LLRAAEESIA ATDARTVEAI
QDIVERSLME QGYFDEAKAY ILYRHRRAEL RTVRADIVAT AVASCDILSC GREPSDASFL
DACLACIQED FPDEPYALSA LSAKFKSFIK ADMSIDERLE SLTRAAVELT TQEAPKWEFI
AARILLFSFR RTLALNCASR GIETFYDKIL WLTDQDLYGA YILQHYTRAE IEEAEGFLRP
ERDELFTYSG LDLLLKRYVI TTRQHVAIES PQEMFLGIAL HLAMEEKNDR MGWVRKFYDM
LSKLEVTMAT PTMSNARKPH HQLSSCFIDT VPDSLDGIYR SIDNFAQVSK FGGGMGMYLG
KVRATGGMIR GFEGAAGGVI RWIRIINDTA VAVDQLGMRA GAAAVYLDAW HKDLPEFLQL
RTNNGDDRMK AHDVFPAVCY PDLFWRLAGE DMGQEWHLMC PHDILTVKGY ALEDYFGDEW
EKRYFDCVAD PRIPKRTMVI RDIVRLVLKS AVETGTPFTF NRDIVNRANP NPHEGIIYCS
NLCTEIAQNM APVESVSVET KTKDGDTVVV TTTRPGDFVV CNLASLSLGR LPVESEEAMR
DVVSTAVRAL DNVIDLNFYA LEYARITNKR YRSIGLGVSG YHHMLAKRGI RWESDEHLAF
ADEVFERINR CAVDASARLA EEKGSYEVFE GSDWQTGAYF DKRDYDGSAW GLVRERAARG
MRNAYLMAVA PTSSTSILAG TTPGVDPIMR RFFLEEKKGG MLPRVAPELS METYWFYKPA
HYIDQTWSVR ASGVRQRHVD QAQSMNLYIT NDYTMRQVFN LYHEAWKAGV KTVYYVRSKS
LEVEECESCA S
//
