ID I3ULG6_9CAUD Unreviewed; 773 AA.
AC I3ULG6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 13-SEP-2023, entry version 28.
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=SWPG_00082 {ECO:0000313|EMBL:AFK66331.1};
OS Synechococcus phage S-CBM2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae.
OX NCBI_TaxID=351708 {ECO:0000313|EMBL:AFK66331.1, ECO:0000313|Proteomes:UP000501889};
RN [1] {ECO:0000313|EMBL:AFK66331.1, ECO:0000313|Proteomes:UP000501889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-CBM2 {ECO:0000313|EMBL:AFK66331.1,
RC ECO:0000313|Proteomes:UP000501889};
RG The Broad Institute Genome Sequencing Platform;
RA Henn M.R., Chen F., Wang K., Levin J., Malboeuf C., Casali M., Russ C.,
RA Lennon N., Chapman S.B., Erlich R., Young S.K., Yandava C., Zeng Q.,
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., Pearson M., Roberts A.,
RA Ryan E., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Synechococcus phage S-CBM2.";
RL Submitted (OCT-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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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; HQ633061; AFK66331.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000501889; 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:UniProtKB-UniPathway.
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:UP000501889}.
FT DOMAIN 9..99
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 773 AA; 87956 MW; 0CDE893826E92956 CRC64;
MEKSMSNGTK VKKRDGRIEH LDLDKMHVMV EEACKDLSGV SASLVEMNSG IQFYDGITTD
EIQQILVKSA ANLITLDTPN YQFVAARLLL YGLRKQVFGK RYEHPDFITH IKRCVDLGVY
DPAILDKYDE QEISHFDSWI DHDRDFLFTY AGLRQVVDKY LVQDRSSGEI YETPQFMYMM
IAATIFQQYP KETRLDYVKR YYDAISKHKI NIPTPIMGGV RTPLRQFASC VLVDVDDTLD
SIFTSDMAIG RYVAQRAGIG INAGRIRGVN SKIRGGEVTH TGVIPFLKKF EATVRCCTQN
GIRGGSATVH FPIWHKEIED IIVLKNNKGT EDNRVRKLDY SIQISKIFYE RFIKNESMHL
FSPHDVPGLY TAFGTDDFDA LYTKYEADPT IPKKSVSAQE LILDLLKERA ETGRVYIMNI
DHCNSHSSFK DQVYMSNLCQ EITLPTDPIG HIDDPDGEIA LCILSAINVG KLKNLDDLEE
LCDLSVRGLE ELIDYQGYPV AAAERATKYR RSLGVGFIGL AHYLAKLGAS YGDNYSLTEV
HKLTEAFQYY LLKSSNQIAR EKGPCEGFER TKYADGILPI DTYKKDVDEL VASAYFYDWE
NLRTSILEHG LRHSTLSAQM PSESSSVVSN ATNGIEPPRD FLSIKKSKKG PLPQIVPQYT
TLKKNYTLLW DMPSNEGYIK IVAVMQKFFD QAISGNWSYN PENYPDNEVP VSVIANDFLT
TYKYGWKTSY YQNTYDNKKD ADVEDNIKRV VELDQLIESI LESEEDDCES CKI
//