ID   VG50_BPML5              Reviewed;         682 AA.
AC   Q05262;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   23-FEB-2022, entry version 92.
DE   RecName: Full=Putative adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE            EC=1.17.4.2;
DE   AltName: Full=Gp50;
GN   Name=50;
OS   Mycobacterium phage L5 (Mycobacteriophage L5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Fromanvirus.
OX   NCBI_TaxID=31757;
OH   NCBI_TaxID=1763; Mycobacterium.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8459766; DOI=10.1111/j.1365-2958.1993.tb01131.x;
RA   Hatfull G.F., Sarkis G.J.;
RT   "DNA sequence, structure and gene expression of mycobacteriophage L5: a
RT   phage system for mycobacterial genetics.";
RL   Mol. Microbiol. 7:395-405(1993).
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   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate
CC       reductase family. {ECO:0000305}.
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DR   EMBL; Z18946; CAA79426.1; -; Genomic_DNA.
DR   PIR; S30995; S30995.
DR   RefSeq; NP_039714.1; NC_001335.1.
DR   SMR; Q05262; -.
DR   GeneID; 2942963; -.
DR   KEGG; vg:2942963; -.
DR   Proteomes; UP000002123; 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; IDA:CACAO.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR040763; RNR_alpha_hel.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep.
DR   Pfam; PF02867; Ribonuc_red_lgC; 2.
DR   Pfam; PF17975; RNR_Alpha; 1.
DR   TIGRFAMs; TIGR02505; RTPR; 1.
PE   3: Inferred from homology;
KW   Cobalamin; Cobalt; Disulfide bond; DNA replication; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..682
FT                   /note="Putative adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000221431"
FT   ACT_SITE        370
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        372
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..381
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   682 AA;  76331 MW;  8D2A71B873BC04A8 CRC64;
     MTDEIPWGPT GELVYNRTYA RTKPDGSKET WPETVERVVD GNLALVDRRH MLEGEREDLV
     RLMTKFKVLP AGRHLWASGV KNAQHLFNCW VAGWPEKISD HFQFTFMRLM EGGGVGANYS
     NHYLEGYPEV VNPLRVEIVC DPEHVDYQAM KDVGILSEHY SHDWAGAYAI EDSREGWAAA
     LVDLIDTHYR PGTVHYQRVY DVSRIRPQGA KLKTFGGVAS GPLPFAVMLQ KVANIFSEYA
     GITLDGIAAM EVDHAIAQCV VAGGVRRSAR MSMMHWDDYQ IDKFINIKAS TGEHWTTNIS
     VEVDDEFWRL AKEGYGSFAV AREDMPKQKR AHRVLKALSE GAVRNGEPGM WDSSLSNVGE
     PNRVVCTNPC GEITLEPWEP CNLGHINLAA FVTPAGKTDY LDLIRAHRLM TRFLIRATFS
     EVADPKSREV LDRNRRIGVG HLGVASYLAL TGSRYSEAPG DKRFTQFLRE MAAEVDSEAE
     RFAHDLRIPV PVKKRTIAPT GTVAKMPGVS EGIHPIFSRY FIRRVRFNLN SDMAELRRLA
     AEGYEIEKDL FAPNTEVVSI PTKDTLVQAV EELGWDEEIV ESADELTLHQ LLAFQALYQM
     CWADNAVSFT ANVHPDAYEA EDVAADLKRF AGLIKGSTIF PESSFPQAPY ERITKQQYES
     AAAKAVEDGV DEECANGACP IK