ID A0A172CIV8_9CAUD Unreviewed; 581 AA.
AC A0A172CIV8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN Name=nrdZ {ECO:0000313|EMBL:ALA12028.1};
GN ORFNames=vB_PaeM_MAG1_048 {ECO:0000313|EMBL:ALA12028.1};
OS Pseudomonas phage vB_PaeM_MAG1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Pakpunavirus; Pakpunavirus MAG1.
OX NCBI_TaxID=1639815 {ECO:0000313|EMBL:ALA12028.1, ECO:0000313|Proteomes:UP000202445};
RN [1] {ECO:0000313|EMBL:ALA12028.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kwiatek M., Parasion S., Miziak L., Gryko R., Lobocka M.B.;
RT "Analysis of the newly isolated bacteriophage vB-PaeM_MAG1 which is able to
RT infect clinical Pseudomonas aeruginosa isolates.";
RL Submitted (APR-2015) 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}.
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DR EMBL; KR052143; ALA12028.1; -; Genomic_DNA.
DR RefSeq; YP_009287344.1; NC_031073.1.
DR GeneID; 29057889; -.
DR KEGG; vg:29057889; -.
DR OrthoDB; 2980at10239; -.
DR Proteomes; UP000202445; 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; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR039718; Rrm1.
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; 3.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003410,
KW ECO:0000313|EMBL:ALA12028.1}.
FT DOMAIN 26..105
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 112..207
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 236..404
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 413..551
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 581 AA; 66621 MW; 58CC519382D90155 CRC64;
MSKRDTFNYS EARKNSQATG ETPLWYTTAG YQLFMKKYSN EGESVRSRFQ AVARAMAQHA
PMVYPEWWDQ DEYTKGKNWE QVFFDVMWDG FVSPSTPLLS NGGLRKKGTT VSCAGGLMDN
NLYDRYNVMT EIAVLTKHSH GTSFSLTNWP SEGDAIRGGE SQGVMPVIRD VINVMEEVAQ
GSRRGSCAYS INPRHGDFWN VIDHLYKRTE SNNVGWLLDD QWCKDMAEKD PETLKRWKRM
MFVKLARGKG YFTFIDKMNR HLAEPFKRAG LRCEASNLCQ ETVLPANDWY TFSCVILNYN
LELYRSWPKH LVFIGQVMSD CNISEYLATM DEVSVQDRRA LEKIYRFTKD FRALGSGVLG
FHTLLQRERF PVGSMDAMFL NNAIFKGMKE QAEACNSWLA KVLGEPTGCR GLGKRNATTM
MMPPTKSTAE LMAGASEGIG LDVAMCFTKQ SAGGEFFRVN KVLLEIIQER GLDWEECARQ
INERKGSVQH VDWLTDHEKA VFRTAFEVRM EDYLRLCSQR QKYIDQGQSI NLYFTSNDSP
AYISYIHRLA MEDPNILSLY YIYSMRGAGD ISRTEECEMC M
//
