ID A0A1B3B117_9CAUD Unreviewed; 687 AA.
AC A0A1B3B117;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=ribonucleoside-triphosphate reductase (thioredoxin) {ECO:0000256|ARBA:ARBA00012275};
DE EC=1.17.4.2 {ECO:0000256|ARBA:ARBA00012275};
GN Name=56 {ECO:0000313|EMBL:AOE44666.1};
GN ORFNames=SEA_REMUS_56 {ECO:0000313|EMBL:AOE44666.1};
OS Gordonia phage Remus.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Soupsvirus; Soupsvirus strosahl.
OX NCBI_TaxID=1887652 {ECO:0000313|EMBL:AOE44666.1, ECO:0000313|Proteomes:UP000202619};
RN [1] {ECO:0000313|EMBL:AOE44666.1, ECO:0000313|Proteomes:UP000202619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Franke B.K., Idrees S., Klinkhammer K.E., Kocina D.M., Lusk T.N.,
RA Notovny A.L., Oberding K.E., Quandt C.A., Schmitz M.Y., Schultz D.E.,
RA Thaoxaochay C., Thomas C.P., Toland T.N., Topel S.A., Warren E.R.,
RA Weber A.J., Welman R.J., Williams K.M., Bonilla J.A., Klyczek K.,
RA Garlena R.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA Hatfull G.F.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC triphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC triphosphate; Xref=Rhea:RHEA:12701, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:61557, ChEBI:CHEBI:61560; EC=1.17.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001283};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate
CC reductase family. {ECO:0000256|ARBA:ARBA00005654}.
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DR EMBL; KX557283; AOE44666.1; -; Genomic_DNA.
DR RefSeq; YP_009281667.1; NC_031031.1.
DR GeneID; 29063860; -.
DR KEGG; vg:29063860; -.
DR OrthoDB; 2980at10239; -.
DR Proteomes; UP000202619; Genome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.20.70.20; -; 1.
DR Gene3D; 3.30.1620.10; b-12 dependent (class ii) ribonucleotide reductase, Chain A, Domain 2; 1.
DR Gene3D; 3.90.1390.10; b-12 dependent (class ii) ribonucleotide reductase, chain A, domain 3; 1.
DR InterPro; IPR040763; RNR_alpha_hel.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep.
DR NCBIfam; TIGR02505; RTPR; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF17975; RNR_Alpha; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613345-2};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000202619}.
FT DOMAIN 9..83
FT /note="Ribonucleotide reductase alpha helical"
FT /evidence="ECO:0000259|Pfam:PF17975"
FT DOMAIN 252..462
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 498..632
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT ACT_SITE 372
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-1"
FT ACT_SITE 374
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-1"
FT DISULFID 93..383
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-2"
SQ SEQUENCE 687 AA; 76623 MW; FBA2D56B03B53C22 CRC64;
MTDTPTNEIP WGPTGELVYN RTYSRTKPDG TKETWPETVA RVVEGNLALV DSKYQIGNER
EDLIRMMTEF KILPAGRHLW ASGVKNAQHL FNCWVSGWPS DISDHFQFTF MRLMEGGGVG
ANYSNRYLEQ YGPVQHFLSV EIVCDPDHAD YQEMKDAGIL SDKYDSEWTG AYPIEDSREG
WASALVDLID THYRADTVNF HRVYDVSRVR PAGAKLKTFG GVASGPKPFA EMLQKVSTIL
SDRSGVKLTG IDAMSIDHAI AQCVVAGGVR RSARMAMMHW ADHQIEEFIN CKQESGDHWT
TNISVEVDEE FWKYASKDPR DEGYGTLVDQ LKAETVLGAL ATGAVRNGEP GMWDSSYSNK
GEPNEVVCTN PCGEITLEPW EPCNLGHINL AAFVTENGRT DHLELLRAHQ LMTRFLIRAT
FSPVGDPKSR EVLDRNRRIG VGHLGVASYL AKTGIRYSMA PQMHSVRGLL RELARKVDDE
AIQFSHDLRI PVPVKKRTIA PTGTVAKMPG VSEGIHPIFS RYFLRRVRFN QNSDFEALAK
LVNEGYEVEE DLFAPNTAVV TIPTKDTLLQ EVTDLYGEDN AEDLVESADE LSLGQLFAFQ
SLYQQLWADN AVSFTANVDP DRYTADDVAD TMQRFAGLIK GSTIFPEASF PQAPYERITK
AQFEAYEAVS IADGVDENCS NGACPIK
//
