ID A0A1B1PA68_9CAUD Unreviewed; 696 AA.
AC A0A1B1PA68;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=ribonucleoside-triphosphate reductase (thioredoxin) {ECO:0000256|ARBA:ARBA00012275};
DE EC=1.17.4.2 {ECO:0000256|ARBA:ARBA00012275};
GN ORFNames=SEA_NANODON_49 {ECO:0000313|EMBL:ANT41053.1};
OS Streptomyces phage Nanodon.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Arquatrovirinae; Likavirus; Likavirus nanodon.
OX NCBI_TaxID=1873777 {ECO:0000313|EMBL:ANT41053.1, ECO:0000313|Proteomes:UP000202682};
RN [1] {ECO:0000313|Proteomes:UP000202682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Adebesin M.O., Ahama K., Alekasir E.M.M., Ali S., Aligholizadeh E.,
RA Allison J.M., Alzaher A., Andaya C.D., Asfaw S., Bansal N., Beauchard M.A.,
RA Betancourt K.A., Bhatia B., Boretti N.A., Brondi J.N., Byrd C.E., Cao A.,
RA Cardosa E.A., Carter A., Chen S., Chen Y., Clara Vega K., Cobuzzi M.,
RA Conn O.L., Crosby I.A., Daly S.B., DePaz I.X., Dhaurali S., Dowdy K.M.,
RA Edokobi N.B., Ekanayake A.B., Ekekwe S.O., Emond M.A., Endres L., Eng S.,
RA Felkoski S.A., Gant C.D., Gaskin B., Gondal S., Gutmann J., Ha T.-A.,
RA Habteyes H., Hariri O., Healey R.M., Heins J.L., Henderson A.L.,
RA Hernandez F.M.D., Hoang P.T., Hope K.T., Husna A., Hussain A., Imani O.,
RA Jackson N.L., Jacob V.M., Kang C., Kantov R.M., Kavuru S., Kerr M.S.-J.E.,
RA Khan O.A., Khan T.M., King T., Kulkarni R., Li A., Maczka C., Maisonet E.,
RA Majethia P.M., Malik D.A., Mariam A., Marquess E.B., Mattison J.,
RA McDonald N., Mehr S., Mengers S.R., Michaels D.P., Mondal S.,
RA Monney de Bebohi F., Nakhleh S.I., Ndubuizu N.C., Nguyen A.H., Nguyen K.M.,
RA Nguyen M.T., Nicholas M.L., Nimalan J.P., O'Connell R.A., Odoi E., Ojo L.,
RA Okoye A.E., Olateru-Olagbegi O., Osei K.V., Osei-Tutu A., Palilla A.M.,
RA Pancholi S., Park J.H.M., Patel K., Patel P., Pennington E., Peterson R.E.,
RA Pon J., Pourkarim H., Reed M.L., Rottman V., Salazar J., Samet S.,
RA Sendze O., Stelmack M.A., Stinnett R., Tchouaga A.L.N., Thompson E.M.,
RA Tran N.G., Truong T., Udo J.A., Verona L.T., Vu T.-Q., Wade J., Wang N.Q.,
RA Waters Z.M., Wellman R.J., Woldegabreal S., Yee A.C., Yirefu M.,
RA Zahangir S., Zhai Y., Devine C.L., Liao K., Prasad P.K., Ruthenberg K.J.,
RA Shonk J.A., Way M., Yousufi H.K., Cao L., Fox J., Hobbs E., Kilic S.,
RA Nunn R., Patel R., Rubenstein M., Erill I., Caruso S.M., Hughes L.E.,
RA Garlena R.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA Hatfull G.F.;
RL Submitted (MAY-2016) 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; KX344445; ANT41053.1; -; Genomic_DNA.
DR RefSeq; YP_009287833.1; NC_031078.1.
DR GeneID; 29080450; -.
DR KEGG; vg:29080450; -.
DR OrthoDB; 2980at10239; -.
DR Proteomes; UP000202682; 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 7..87
FT /note="Ribonucleotide reductase alpha helical"
FT /evidence="ECO:0000259|Pfam:PF17975"
FT DOMAIN 348..492
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 504..652
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT ACT_SITE 378
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-1"
FT ACT_SITE 380
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-1"
FT DISULFID 97..389
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-2"
SQ SEQUENCE 696 AA; 77334 MW; 95910FE06F510900 CRC64;
MTDTNQVPFG PTGQLVYERT YSRTLADGSK ETWPDTVRRV AKGNLALVHG SDMNAWSQAV
KDEYDELVSF MDVFAIIPAG RHLWATGVKG RQYLFNCHVA PWGEKLSRHF EFTFMRLMEG
GGVGGNYSSS YLQGYGAPRR ELDVHIVCDS THPDFEEMKS LGILSTEYDS DWDGAFEVED
SREGWAAAMV DLIDTFMTDG EVIHRNRVYD VSRVRAKGAR LKTFGGTASG PAPFGRMMQE
IGRILSKAAR EVGEWAVHPH VTPTEAMEID HAIAECVVSG GVRRSARMAI VKWDDPFIED
FLACKHDMSK HWTTNISVEI DYRFMKALND PQHGLHAEAV AVHRKVVEGM LINGEPGYWN
SSYSNEGEVG TVIATNPCGE IALEPTENCN LGHVNLDYFA PTEKGGGIQK GKLLRAHQLM
TRFLMRATYG DVTDAEQAAK LAANRRIGVG HLGVQGFLAK QGVRYSSAPY VESFRWLLED
LYDAVREEAR EYAFQLRIPE PVKVTTVAPT GSIAKLPGVS EGIHPIYARH FLRRVRFSMP
DPAQAATVQK AVEDGNLVEQ CIYDQSGNTM VVAYPTKEKL VAEVEAMGFD PEVVESADEI
PLDAMLAFQA MYQTYYADNA VSFTVNFPEG QYDVDEAADI IRGWLPELKG TTLMPDGTRA
QAPYERLTAE QFAEYEVFST EDSTDENCAN GACPVR
//
