ID R6UE81_9FIRM Unreviewed; 838 AA.
AC R6UE81;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BN746_02791 {ECO:0000313|EMBL:CDC84018.1};
OS Erysipelotrichaceae bacterium CAG:64.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=1262981 {ECO:0000313|EMBL:CDC84018.1, ECO:0000313|Proteomes:UP000018179};
RN [1] {ECO:0000313|EMBL:CDC84018.1, ECO:0000313|Proteomes:UP000018179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:64 {ECO:0000313|Proteomes:UP000018179};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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:CDC84018.1}.
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DR EMBL; CBGA010000074; CDC84018.1; -; Genomic_DNA.
DR AlphaFoldDB; R6UE81; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000018179; 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}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 838 AA; 96791 MW; 10A86CB61ED19528 CRC64;
MKIQKRDGQL QEFEGEKIAQ AIRKAFSSTG TLIEESVLKE 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
//
