ID   VG50_BPMD2              Reviewed;         693 AA.
AC   O64240;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   13-SEP-2023, 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 D29 (Mycobacteriophage D29).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Fromanvirus.
OX   NCBI_TaxID=28369;
OH   NCBI_TaxID=1763; Mycobacterium.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9636706; DOI=10.1006/jmbi.1997.1610;
RA   Ford M.E., Sarkis G.J., Belanger A.E., Hendrix R.W., Hatfull G.F.;
RT   "Genome structure of mycobacteriophage D29: implications for phage
RT   evolution.";
RL   J. Mol. Biol. 279:143-164(1998).
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; AF022214; AAC18490.1; -; Genomic_DNA.
DR   PIR; G72805; G72805.
DR   RefSeq; NP_046865.1; NC_001900.1.
DR   SMR; O64240; -.
DR   GeneID; 1261592; -.
DR   KEGG; vg:1261592; -.
DR   OrthoDB; 2980at10239; -.
DR   Proteomes; UP000002131; Segment.
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; 1.
DR   Pfam; PF17975; RNR_Alpha; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE   3: Inferred from homology;
KW   Cobalamin; Cobalt; Disulfide bond; DNA replication; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..693
FT                   /note="Putative adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000221430"
FT   ACT_SITE        375
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        377
FT                   /evidence="ECO:0000250"
FT   DISULFID        90..386
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   693 AA;  77250 MW;  148B752C15EC561F CRC64;
     MTEGEIPWGP TGELVYNRTY SRVKPDGTRE TWPETVERVV SGNLALVDSR YQLPGEREDL
     LRLMREFKIL PAGRHLWASG VKNAQHLFNC WVSGWTEKPS DHFEFTFMRL MEGGGVGANY
     SNRFLADYPH VKQELEVHIV CDEDHDDYAD LAEAGQLSSR YDSDWVDAFV IEDSREGWAA
     ALVDLIDTHY RDDVAHKERV YDVSRVRAAG RKLKTFGGTA SGPVPLAKML TEVSEILSRC
     AREGEQYRFE DGGALTGLDA MEIDHAIAQC VVAGGVRRSA RMAMMHWADW QVETFTNIKQ
     DSGSHWTTNI SVEVDDAFWS LAKAPVDPLN PRSTKAHRVL KALSEGAVRN GEPGMWDSSL
     SNVGEPNEVV CTNPCGEITL EPWEPCNLGH INLAAFVTDA GKTDYIDLIR AHRLMTRFLI
     RATFSAVADP KSREVLDRNR RIGVGHLGVA SYLALTGRRY SQAPGDKRFT AFLREMAAEV
     DRAAEEFSHE LRIPVPVKKR TVAPTGTIAK MPGVSEGIHP IFSRYFIRRI RFSVLDNDQF
     LTASQYAADG YHVEKDQYDK SGNTWVVEIP TKDTLVEAVA ARFGRDAEDI VESANELTLH
     QLLAFQALYQ TCWADNAVSF TANVDPDAYE GVDVAADLQR FSGLIKGSTI FPEESFPQAP
     YERITKQQYE AAAIKAVADG VDEECANGAC PIK
//