ID R4PMY9_9BACT Unreviewed; 803 AA.
AC R4PMY9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-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 Name=nrdA {ECO:0000313|EMBL:AGL62274.1};
GN ORFNames=L336_0571 {ECO:0000313|EMBL:AGL62274.1};
OS Candidatus Saccharimonas aalborgensis.
OC Bacteria; Candidatus Saccharibacteria; Candidatus Saccharimonadia;
OC Candidatus Saccharimonadales; Candidatus Saccharimonadaceae; Saccharimonas.
OX NCBI_TaxID=1332188 {ECO:0000313|EMBL:AGL62274.1, ECO:0000313|Proteomes:UP000013893};
RN [1] {ECO:0000313|EMBL:AGL62274.1, ECO:0000313|Proteomes:UP000013893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM71 {ECO:0000313|EMBL:AGL62274.1};
RX PubMed=23707974; DOI=10.1038/nbt.2579;
RA Albertsen M., Hugenholtz P., Skarshewski A., Nielsen K.L., Tyson G.W.,
RA Nielsen P.H.;
RT "Genome sequences of rare, uncultured bacteria obtained by differential
RT coverage binning of multiple metagenomes.";
RL Nat. Biotechnol. 31:533-538(2013).
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; CP005957; AGL62274.1; -; Genomic_DNA.
DR AlphaFoldDB; R4PMY9; -.
DR STRING; 1332188.L336_0571; -.
DR KEGG; saal:L336_0571; -.
DR PATRIC; fig|1332188.3.peg.560; -.
DR HOGENOM; CLU_000404_3_0_0; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000013893; 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 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:UP000013893}.
FT DOMAIN 4..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 803 AA; 90045 MW; 1159F3F3A4001694 CRC64;
MNGIHVVKRD GTREPFDANK INLALVKASE GLPDQIQKVV QVATELQLTL FDGITSEELD
EAVIHTALQN VKDDPDFDTI AARLLLKNVY KNILGDYKDD AELKKLHEKA FPQYLKTAVK
EGLLDKRMVD PALFDVKKLA AALDPQRDAL SKYLGVITNK NRYALRKQNG EPVETPQFTH
MRIAMGLSFN EKDPTAAALD FYRHMSNLDY LPGGSTRVNA GGSFPQLSNC FVIDVDDDME
AIAKSIRDTM WIAKGTGGIG ISMNKLRAAG SPVKTTNTVS TGPLPFMKMI DTALFAVSRK
GKKAGAAAIY MENWHVNFPG FMELRQNSGD PYFRTRFANI AVYISDEFMR RVQKEQDWYM
FDPAETPDLS ELYGDAFAKR YNEYVKLAKA GKLREFKTVP ARQQWRQILT SLQASSHPWI
TWKDTINVRA LNNNRSTIHS SNLCTEITLP NDEKNISVCN LVSINLSAFL DVDKKVWDWK
RLEAATRSAI RQLDNLCDIT DTPIPEAINS IQTTRALGLG IMGFTDVIEK LGYSYESEEA
YDTMDQLAEY ISYYAIDESA ELAKTRGSYP DFKGSGWSKG QLPIDTVDAL AKDRSVAVDV
TRKTRLDWEA LRKKTTKGMR NATLMAIAPT ANIAHVAGTT PGIDPQFGQI FSRSTLNGKF
LEVNTNLVRD LKALGIWNEV KDQLLIEQGD LTNIDTVPQH LKDVYKTCFQ LSPFAFVEVA
ARAQKWVDQA ISRNMYLESR SIDDMEKVYM GAWKRGLKTT YYLHMKPRHQ AELSTVKVNK
ADAIVDSSGA RKSGFGFAKK QAA
//
