ID A0A2Z4Q201_9CAUD Unreviewed; 681 AA.
AC A0A2Z4Q201;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=ribonucleoside-triphosphate reductase (thioredoxin) {ECO:0000256|ARBA:ARBA00012275};
DE EC=1.17.4.2 {ECO:0000256|ARBA:ARBA00012275};
GN Name=41 {ECO:0000313|EMBL:AWY04053.1};
GN ORFNames=SEA_SHUMAN_41 {ECO:0000313|EMBL:AWY04053.1};
OS Rhodococcus phage Shuman.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Rerduovirus.
OX NCBI_TaxID=2234034 {ECO:0000313|EMBL:AWY04053.1, ECO:0000313|Proteomes:UP000250908};
RN [1] {ECO:0000313|EMBL:AWY04053.1, ECO:0000313|Proteomes:UP000250908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Washington J.M., Teetzmann A., Kanai K., Rolling C., Souza S., Dukehart C.,
RA Peter P.J., Zapata J., Garlena R.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (MAY-2018) 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; MH316569; AWY04053.1; -; Genomic_DNA.
DR Proteomes; UP000250908; 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; 3.
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 5..81
FT /note="Ribonucleotide reductase alpha helical"
FT /evidence="ECO:0000259|Pfam:PF17975"
FT DOMAIN 251..319
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 323..456
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 488..626
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT ACT_SITE 364
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-1"
FT ACT_SITE 366
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-1"
FT DISULFID 91..375
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR613345-2"
SQ SEQUENCE 681 AA; 76321 MW; 29DDBE793B3638EA CRC64;
MTIDEPINWG PQGELVYNRT YSRPKPDGTK ETWPETVERV VDGNLGLVDE RYHAPYERDE
LIEMIRDFKI LPAGRHLWAS GVKGRQYLFN CHVSHWNEKL SDHFEFTFMR LMEGGGVGAN
YSNIYLSQYP EVQQTLSVEI VCDPSHPDYA ELEQAGVLSK RYNSDWVGAY EVEDSREGWS
GSLVELVDTF YRDVVEHTYR VFDVSRVRGR GTRLKTFGGT ASGPLPLAKM LMDVADVLND
FTGQKLTGLG AMEIDHHLAE CVVSGGNRRS ARMAMMRWDD PQIFEFIHCK AQSGKHWTTN
ISVEVDQRFW NNADDDEDTD MGVHAKKVLA EISKGALNNG EPGTWNSDLS NDGEVERAVC
TNPCGEIALT PWENCNLGHV NLAAFVDDTG HVDTIGLYRA HRLVARFLIR ATFGDVNDPK
QQDQLARQRR IGVGHLGVAS HLALRGIRYS DAPANEDFRE ELRIYRFLVQ SEARDYAHQL
RIPTPIKTTT VAPTGTIAKM PGVSEGIHPI FSRYFIRRIR FSVVDPEQAA TLATYRMMGY
SVEPCEYAAN TDVVAIPTKD SLVADVAAIY GEEKAEEIVQ SADELTLEEM LAFQALYQVS
YADNAVSFTA NLDPTKYTTD QVGEILQDFA PLLKGTTIFP DASMPQAPYE RLTREQYEEA
VAKEIGDGVD ENCANGACPI K
//
