ID R9TQ88_9CAUD Unreviewed; 769 AA.
AC R9TQ88;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=SWYG_00160 {ECO:0000313|EMBL:AGN33669.1};
OS Synechococcus phage S-IOM18.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae; Tefnutvirus; Tefnutvirus siom18.
OX NCBI_TaxID=754039 {ECO:0000313|EMBL:AGN33669.1, ECO:0000313|Proteomes:UP000204294};
RN [1] {ECO:0000313|EMBL:AGN33669.1, ECO:0000313|Proteomes:UP000204294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-IOM18 {ECO:0000313|EMBL:AGN33669.1,
RC ECO:0000313|Proteomes:UP000204294};
RG The Broad Institute Genome Sequencing Platform;
RA Henn M.R., Clokie M., Levin J., Malboeuf C., Casali M., Russ C., Lennon N.,
RA Chapman S.B., Erlich R., Young S.K., Yandava C., Zeng Q., Fitzgerald M.F.,
RA Alvarado L., Anderson S., Berlin A., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Green L., Griggs A., Gujja S., Heilman E.R., Heiman D.,
RA Hollinger A., Howarth C., Larson L., Mehta T., Neiman D., Pearson M.,
RA Roberts A., Ryan E., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., White J., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Synechococcus phage S-IOM18.";
RL Submitted (SEP-2010) 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|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HQ317383; AGN33669.1; -; Genomic_DNA.
DR RefSeq; YP_008126483.1; NC_021536.1.
DR GeneID; 16045474; -.
DR KEGG; vg:16045474; -.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000204294; Genome.
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:UP000204294}.
FT DOMAIN 8..98
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 769 AA; 87387 MW; AA460010E4A66592 CRC64;
MEKGMKEIHV IKRDGEQEPL NLDKIHVMVE HACNGLAGVS ESQVEMNAGL QFFDGIKTSD
IQEILVRSAN DLISLEAPNY QFVAARLLLF GLRKAVYNGH PDGHPPLKEH VEKCIERSVY
DSSILTKYTD EEWEKLSSFM DHDRDYLFTY AGIRQVVDKY LVQDRSSGEV YETPQFMYMM
IAATLFQDDD KFYRLEYVKK YYDAISKHRI NIPTPVMAGV RTPLRQFASC VLVDVDDTLD
SIFSSDMAIG YYVAQRAGIG INAGRIRGIN SKIRDGEVQH TGVVPFLKKF ESTVRCCTQN
GIRGGSATVH FPIWHQEIED IIVLKNNKGT EDNRVRKLDY SIQISKLFYE RFISNGIISL
FSPHDVPGLY DAFGTDSFDS LYVEYESDKS IPRNTVKAQE LFLSILKERA ETGRLYIMNI
DHCNSHSSFK DKVNMSNLCQ EITLPTDPIQ HIDRSGEIAL CILSAINVGK LKSLDELDEL
CDLAVRGLDA LIDYQEYPVS AARESTINRR SLGIGYIGLA HYLAKHGANY DSTKAHDLVH
KLTERFQYAL LNASNRLAME KGPCGYFGKT KYSDGVLPID TYKKEVDEIV PNELQCDWEY
LRERIKQYGL RNSTLSAQMP SESSSVVSNA TNGIEPPRAY LSIKKSKKGP LKQIVPSYTT
LKNAYTLLWD MPNNDGYIKV TSVIQKFFDQ AISGNWSYNP EMYPDNEVPV SVMAKDLLTT
YKYGWKTSYY QNTYDAKKDG DDEPAKENVD ELIQQLLESE EEDCESCKI
//
