ID Q21T47_ALBFT Unreviewed; 981 AA.
AC Q21T47;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
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=Rfer_3347 {ECO:0000313|EMBL:ABD71056.1};
OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS (Rhodoferax ferrireducens).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=338969 {ECO:0000313|EMBL:ABD71056.1, ECO:0000313|Proteomes:UP000008332};
RN [1] {ECO:0000313|Proteomes:UP000008332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-621 / DSM 15236 / T118
RC {ECO:0000313|Proteomes:UP000008332};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL Submitted (FEB-2006) 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; CP000267; ABD71056.1; -; Genomic_DNA.
DR AlphaFoldDB; Q21T47; -.
DR STRING; 338969.Rfer_3347; -.
DR KEGG; rfr:Rfer_3347; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_4; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008332; Chromosome.
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; 2.
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:UP000008332}.
FT DOMAIN 35..135
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 149..238
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 981 AA; 108535 MW; B2F68E1A9E6D892D CRC64;
MQTVSNPSPA RHSDVPAVHR MDGIDDTAAH SLSQYQIIRR NGAVVPFEPN KIAVAMMKAF
LAVHGTQGAA SASVRESVDG LTQGVIHALM RSRPAGGTFH IEDVQDQVEL GLMRGGHHEV
ARAYVLYREK RTQERAQQLI ATAATAPLLH VVDKGGRIVL DLARLKGIIE SACAGLGADI
KPEPILAETM RNLYDGVPME EVYKASILAA RTLIEKDPDY TYATARLLFH TIANEVLGRD
VVQADMAQAY VDYFPQFIKK GIDHELLDER LQQFDLQRLG AALKAERDLK FDYLGLQTLY
DRYFLHVGKA RIELPQAFFM RVAMGLSLGE IDREARAIEF YEVLSSFDFM SSTPTLFNSG
TLRSQLSSCY LTTVPDDLDG IYESIKENAL LSKFAGGLGN DWTRVRALGA HIKGTNGESQ
GVVPFLKVVN DTAVAVNQGG KRKGAVCTYL ETWHLDIEEF LELRKNTGDD RRRTHDMNTA
NWVPDLFMRR VMEKGQWTLF SPNNVPDLHD KFGADFEKAY VAYEEKAARG EIRPARTVQA
ADLWRKMLTM LFETGHPWIT FKDACNIRSP QQHVGVVHSS NLCTEITLNT SDTETAVCNL
GSVNLLQHLK NAPAGSADGA KVLDHAKLQK TITTAMRMLD NVIDINFYAV KKARDANMRH
RPVGLGVMAF QDSLYELRIP YASDAAVAFA DTSMEAICYY AYWASTELAR ERGQYTSYKG
SLWDQGILPI DTLDMLARER GGYVEVDRSS TLDWEALRKK IAKDGMRNSN CTAIAPTATI
SNIIGVDASI EPCFGNLSVK SNLSGEFTII NSYLVQDLKR LGLWDDVMVM DLKHFDGSLN
PIDRVPADVK ALYATAFEIE TRWLVEAAAR RQKWIDQAQS LNIYMGGASG KKLDDTYKLA
WIRGLKTTYY LRTMSATHAE KSTVTAGRMN AVSSGSESAH GGASMSALDA AAATARMQMA
SGPATDIKFC GVDDPTCESC Q
//
