ID   VG50_BPMB2              Reviewed;         672 AA.
AC   Q857H2;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   13-SEP-2023, entry version 78.
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 Bxz2 (Mycobacteriophage Bxz2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Microwolfvirus.
OX   NCBI_TaxID=205870;
OH   NCBI_TaxID=1763; Mycobacterium.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12705866; DOI=10.1016/s0092-8674(03)00233-2;
RA   Pedulla M.L., Ford M.E., Houtz J.M., Karthikeyan T., Wadsworth C.,
RA   Lewis J.A., Jacobs-Sera D., Falbo J., Gross J., Pannunzio N.R., Brucker W.,
RA   Kumar V., Kandasamy J., Keenan L., Bardarov S., Kriakov J., Lawrence J.G.,
RA   Jacobs W.R. Jr., Hendrix R.W., Hatfull G.F.;
RT   "Origins of highly mosaic mycobacteriophage genomes.";
RL   Cell 113:171-182(2003).
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; AY129332; AAN01804.1; -; Genomic_DNA.
DR   RefSeq; NP_817639.1; NC_004682.1.
DR   SMR; Q857H2; -.
DR   GeneID; 1259263; -.
DR   KEGG; vg:1259263; -.
DR   OrthoDB; 2980at10239; -.
DR   Proteomes; UP000000729; 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; 3.
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..672
FT                   /note="Putative adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000221429"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..367
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   672 AA;  75158 MW;  F1C8F1FFBEA25E12 CRC64;
     MTNWGPTGEL VYNRTYSRTK PDGSKETWPE TVRRVVDGNL ALVDERYHLP GERADLIRLM
     EEFKILPGGR HLWASGVKNA QHLFNCWVSG WTEKPSDHFE FTFMRLMEGG GVGANYSNRF
     IDYGPVQQEL YVHIVCDPDH PDYEAMKEAG VLSTEYDPDW AGAFVIEDSR EGWAAALVDL
     IDTHYRDEVS HFQRVYDVSR VRQFGAKLKT FGGTASGPLP LARMLIDVCE ILSEIATEGG
     QLTGIAAMEI DHAIAQCVVA GGVRRSARMS MMHWKDPQVY EFLRIKQDTG SHWTTNISLE
     VDDEFWVAVE EGWAGPNNRI LRELTEGMVA NGEPGFWNSS LSNVGEPNEV VCTNPCGEIT
     LEPWEPCNLG HVNLAAFAHG NGSYDITGLY RAHRLVTRFL MRATFSPVAD PKSREVLDRN
     RRIGVGHLGV ASFLALCGWK YSEARTNEEF KWLLRSLAEE VDHAATQFAH QLRIPVPVKK
     RTVAPTGTIA KMPGVSEGIH PIFSRYFIRR VRLSMSDPDQ TRMLADYGRQ GYEVEDDLYA
     KFTGVVSIPT QDTLVAEVIE HYGQDSESLV ESAADLSLNE LLGFQALYQT IWADNAVSFT
     ANVDPETYNA DDVRQQLRLF GGLLKGATIF PEASMPQAPY ERITKEQYEQ ATAKAVADGV
     DEDCANGACP IR
//