ID A0A411B585_9CAUD Unreviewed; 704 AA.
AC A0A411B585;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ribonucleoside-triphosphate reductase (thioredoxin) {ECO:0000256|ARBA:ARBA00012275};
DE EC=1.17.4.2 {ECO:0000256|ARBA:ARBA00012275};
GN Name=50 {ECO:0000313|EMBL:QAX95499.1};
GN ORFNames=SEA_BARTHOLOMEWSD_50 {ECO:0000313|EMBL:QAX95499.1};
OS Streptomyces phage BartholomewSD.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Arquatrovirinae; Caelumvirus.
OX NCBI_TaxID=2510587 {ECO:0000313|EMBL:QAX95499.1, ECO:0000313|Proteomes:UP000289364};
RN [1] {ECO:0000313|EMBL:QAX95499.1, ECO:0000313|Proteomes:UP000289364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Fujii Q., Erb M.L., Fernandez L.A., Trigg S., Khanna K., Pogliano K.,
RA Pogliano J., Garlena R.A., Russell D.A., Pope W.H., Jacobs-Sera D.,
RA Hatfull G.F.;
RL Submitted (JAN-2019) 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; MK460245; QAX95499.1; -; Genomic_DNA.
DR Proteomes; UP000289364; 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}.
FT DOMAIN 6..84
FT /note="Ribonucleotide reductase alpha helical"
FT /evidence="ECO:0000259|Pfam:PF17975"
FT DOMAIN 350..486
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 512..660
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 684..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-1"
FT ACT_SITE 388
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-1"
FT DISULFID 94..397
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-2"
SQ SEQUENCE 704 AA; 78256 MW; 8B9D46528EE8EA03 CRC64;
MSNVPFGPTG ELVYNRTYSR TLADGSKETW PDTVRRVAAG NLALVHGTDQ TAWSEAVRAE
YDELVSYMDE FAIIPAGRHL WATGVKGRQY LFNCHVAPWG DRLSRHFEFT FMRLMEGGGV
GGNYSSSYLR EYGAPRRKLE VHVVCDPMHQ DYEEMKAAGL LSTEYDSDWA GAFEVEDSRE
GWADALVDLI DTFMTDEPVK HKQRVYDVSR VRCKGSRLKT FGGTASGPGP FARMLQEVAV
VLNGAVGDRH VEVGDGFGWG YEHLTPVEAM EIDHAIAECV VSGGVRRSAR MAICKWNDPF
IDAFLDCKAD GSKHWTTNIS VEIDQDFLGY LSGDKIDDFG PGGNEMAWHV HRKVVEGMLR
NGEPGYWNST YSNEGEVNPV IATNPCGEIA LPETGACVLG HVNMDHFAPK GKGGLPDFKG
LYRAHELMTR FLIRATYGDM TDDQQREVMH SERRVGVGHL GVQGYLAKLG IRYSNAPYNE
PFRVLLRNLY DAVRDEAREY AFQLRVPEPV KVTTVAPTGS IAKLPGVSEG IHPIYARYFL
RRVRFSMTDP AQAATVQDAV NAGHLVEKCI YDQSGNTMVV AYPTKEKLVA EVEALGYDPA
IVESADEIDL NAMLAFQAMY QEEYADNAVS FTVNFPEGKY TVDEAADIIE SWLPELKGTT
LMPDGTREQA PYERLSAERF AEYEVTSVED STDEECSTGA CPVR
//
