VG50_BPMB2
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 12-AUG-2020, entry version 75.
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 Caudovirales; Siphoviridae; Fromanvirus.
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 Proteomes; UP000000729; 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 InterPro; IPR040763; RNR_alpha_hel.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep.
DR Pfam; PF02867; Ribonuc_red_lgC; 3.
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..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
