ID A0A222ZQ84_9CAUD Unreviewed; 674 AA.
AC A0A222ZQ84;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=ribonucleoside-triphosphate reductase (thioredoxin) {ECO:0000256|ARBA:ARBA00012275};
DE EC=1.17.4.2 {ECO:0000256|ARBA:ARBA00012275};
GN Name=50 {ECO:0000313|EMBL:ASR86688.1};
GN ORFNames=SEA_ET2BRUTUS_50 {ECO:0000313|EMBL:ASR86688.1};
OS Mycobacterium phage Et2Brutus.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Fromanvirus.
OX NCBI_TaxID=2015881 {ECO:0000313|EMBL:ASR86688.1, ECO:0000313|Proteomes:UP000226307};
RN [1] {ECO:0000313|Proteomes:UP000226307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alkhairo H., Bobbity S., Brown S., Diesel V., Dunn T., Grim D., Headen C.,
RA Izadpanah P., Khan L., Kiflezghi M., Kindberg J., Park S., Pokhrel S.,
RA Sanders W., Johnson A., Stoner T.H., Garlena R.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hatfull G.F.;
RL Submitted (MAY-2017) 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; MF140410; ASR86688.1; -; Genomic_DNA.
DR Proteomes; UP000226307; 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 6..78
FT /note="Ribonucleotide reductase alpha helical"
FT /evidence="ECO:0000259|Pfam:PF17975"
FT DOMAIN 322..451
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 485..628
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT ACT_SITE 359
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-1"
FT ACT_SITE 361
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-1"
FT DISULFID 88..370
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-2"
SQ SEQUENCE 674 AA; 75586 MW; 1BC957663B7CAA3E CRC64;
MSEIPWGPTG ELVYKRTYSR VKPDGSHEEW PDTVRRVVEG NLALVPARYQ LDGEREDLIR
LMSEFKILPA GRHLWASGVK GAQHLFNCWV AGWPDKISEH FEFTFMRLME GGGVGANYSN
HFLEGYPEVV HPLKVEIVCD PDHVDYQAMK DAGILSEHYS HDWVGAYAIE DSREGWAAAL
VDLIDTHYRP DTVHFQRVYD VSRIRPQGAK LKTFGGVASG PLPFAVMLQK VAEILSDRAG
TVLTGLDAMA IDHAIAECVV AGGVRRSARM SMMHWDDPQI WEFLKCKQDT GSHWTTNISV
EVDDEFWHHI NTEGPRPAWP GDVLKAISEG ALRNGEPGMW DSSVSNVGEP NRVVCTNPCG
EITLEPWEPC NLGHINLAAF VKDNGKVDQL DLYRAHELMT RFLIRATFSE VADPKSREVL
DRNRRIGVGH LGVASFLAMT GRKYSDAPLD RRFKQTLREL SGVVDQAAEK FCHELRIPVP
VKKRTVAPTG TVAKLAGVSE GIHPIFSRYF NRRVRFNINS DSEELAKLEA QGYHVEDDLY
APNTKVVTIP TKDTLVQAVA DLYGDHRAEE LVESVDEISL HDLIAFQAMY QTCWADNAVS
FTANVDPDQY RPEDVEEELT RFSGWIKGST IFPEKSFPQP PYERITKQQY EEAVAKAVSD
GVDENCANGA CPIK
//
