ID Q47KI8_THEFY Unreviewed; 821 AA.
AC Q47KI8;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 121.
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 OrderedLocusNames=Tfu_3001 {ECO:0000313|EMBL:AAZ57034.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ57034.1};
RN [1] {ECO:0000313|EMBL:AAZ57034.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ57034.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) 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}.
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DR EMBL; CP000088; AAZ57034.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47KI8; -.
DR STRING; 269800.Tfu_3001; -.
DR KEGG; tfu:Tfu_3001; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_11; -.
DR UniPathway; UPA00326; -.
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; 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..76
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 772..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 91691 MW; 345380DA4B0A8491 CRC64;
MERIRKVVAE ACQGLPGASA ETVIAEATRG FYPGITPAEL ELALIMAART FVETDPDYSY
VSARLLLDKL RREALTFLSG HPDEATHADM ARRYPEYLRA FITRGIELEH LTPELADFDL
DRLGAALRPE RDLNFTYLGL QTLYDRYFLH HEGTRYELPQ AFLMRVAMGV ALHEDDRNAR
AIEFYELLSS FDFMCSTPTL FNAGTRRPQL SSCFLTTVGD DLAEIFRAIS NNALLSKYSG
GLGNDWTPVR GLGAHIKGTN GKSQGVVPFL KIANDTAVAV NQGGKRKGAV CAYLETWHID
IEEFLDLRKN TGDERRRTHD MNTANWVPDL FLERVESDAQ WTLFSPDEVP DLHDRYGEDF
ARAYVAYERA ADRGEIRVFR RVRAVDLWRR MLTMLFETGH PWITFKDPCN LRSPQQHAGV
VHSSNLCTEI TLNTSLDEVA VCNLGSVNLA NHVGPDGLDA ERLRRTVRTA VRMLDNVIDV
NLYTIPEAER ANMRHRPIGL GLMGYQDALF TLRLPVASPE AVEFADESME LLSYYAIEAS
ADLAAERGSY SSFEGSLWSR GILPIDSLEL LAEARRGDLD VDRTQRLDWD TLREKVRTTG
MRNSNVMAIA PTATIANIVG VNPSIEPLYR NLYVKANMSG DFTVVNPSLV RDLKERGLWD
EEMVTALKLH DGSLGPIDRV PEDLKNLYAT AFEIDPIWLV DAASRRQKWI DQAQSLNLYM
AEPSGRKLDE LYRRAWRKGL KTTYYLRSQG ATHVEKSTLR GTDGRLNAVT PVAVSAPSPS
PTPAPRPAAA PPRSAAGPAP DLTAEAAAFC AVDDPECEAC Q
//
