ID X2JMV9_9CAUD Unreviewed; 779 AA.
AC X2JMV9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=Bcp1_122 {ECO:0000313|EMBL:AHN66597.1};
OS Bacillus phage Bcp1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Herelleviridae; Bastillevirinae; Caeruleovirus; Caeruleovirus Bcp1.
OX NCBI_TaxID=584892 {ECO:0000313|EMBL:AHN66597.1, ECO:0000313|Proteomes:UP000019744};
RN [1] {ECO:0000313|EMBL:AHN66597.1, ECO:0000313|Proteomes:UP000019744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24926042;
RA Schuch R., Pelzek A.J., Fazzini M.M., Nelson D.C., Fischetti V.A.;
RT "Complete Genome Sequence of Bacillus cereus Sensu Lato Bacteriophage
RT Bcp1.";
RL Genome Announc. 2:e00334-e00314(2014).
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}.
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DR EMBL; KJ451625; AHN66597.1; -; Genomic_DNA.
DR RefSeq; YP_009031403.1; NC_024137.1.
DR GeneID; 19487329; -.
DR KEGG; vg:19487329; -.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000019744; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
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.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000019744}.
FT DOMAIN 175..229
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 232..762
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 779 AA; 88561 MW; E1AC3B1BC75B4964 CRC64;
MAEVQIINRG NFIEFYDPKK VENYLRRYTP EGVNVNSIVG SVTEFVELEE NVTSLKIQQE
LYSITEGLIS VRESYWQDVA GCIKADILRK EVYNNRGFET GLKRVLELGY EGEQYADFFK
KYSDEEIAEL EKHINEDNDY FVNHVGVHIA YDRYTTSVPV KKEQNGKEIT VGVKKIETLQ
ERYMIVSMFL HQNETKDRIA KVIRGYNRTG ATDFTPATPT FMNSGRPNGN LSSCFVGMTD
DSLDDIYREA DQFAKVSKNA GGYGLYFGKV RSLGSSIRKK PGLSSGAVPF MKLFDVTAGT
VDQQSKRPGA VTITLDVWHR DTSSFLKTPL DNTVLEKQMH KIFLAVSLPD LFFRKLQKNE
QWYQFDPKEV QDIMGWGLED CYDERKDGGT FSERYEQCVQ AYKAGHLQLV TITNPLTILA
EINKTRIEKG HPFLFFRDAV NRDNANGGMI YCSNLCTEIA IPMSTPAIVT EKIKKDGEDI
MVQYTRPGDI PTCNLSSTNL SKVAKVRIAG GDWRAYLAEL IPVQYRMLAN VVLLNEQDEM
PQTKISSLRK REVGLGTMGL AHALAISHIA IDSEKALEWQ NEVFEEIAYQ VIKASMELAK
ETGDIAPHFP KTKWADGSYI EYKFKAHSED KERWEALKQD IIKYGLYSTI HMATAPTETI
SYIANTTAGN DPIYGKEYTL EKAGIKTNMV APGIGMDNIF YYKDAFIIKK DMFLKGVGIR
QRWIDQSIST NLYYIKDNLQ AFDMIQDYIT AWKEGAKTIY YHRSQTTKAY ELACESCAG
//
