ID   A5V205_ROSS1            Unreviewed;       768 AA.
AC   A5V205;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=ribonucleoside-triphosphate reductase (thioredoxin) {ECO:0000256|ARBA:ARBA00012275};
DE            EC=1.17.4.2 {ECO:0000256|ARBA:ARBA00012275};
GN   OrderedLocusNames=RoseRS_4577 {ECO:0000313|EMBL:ABQ92908.1};
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ92908.1, ECO:0000313|Proteomes:UP000006554};
RN   [1] {ECO:0000313|Proteomes:UP000006554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Roseiflexus sp. RS-1.";
RL   Submitted (APR-2007) 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; CP000686; ABQ92908.1; -; Genomic_DNA.
DR   RefSeq; WP_011959245.1; NC_009523.1.
DR   AlphaFoldDB; A5V205; -.
DR   STRING; 357808.RoseRS_4577; -.
DR   KEGG; rrs:RoseRS_4577; -.
DR   eggNOG; COG0209; Bacteria.
DR   eggNOG; COG1327; Bacteria.
DR   HOGENOM; CLU_002384_0_0_0; -.
DR   OrthoDB; 9763270at2; -.
DR   Proteomes; UP000006554; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; -; 2.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR040763; RNR_alpha_hel.
DR   PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   Pfam; PF17975; RNR_Alpha; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00492}; Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABQ92908.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT   DOMAIN          28..120
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   768 AA;  87176 MW;  FD060D1E4FC42098 CRC64;
     MTQSNTEFNG TRSNGSTDTL HPDVVVPTMI IKRDGRVVPF DVSRIENAMA RCFASFGRIP
     DTPIPELAQR VVNIVAARLQ GRPPTVEGVQ DIVEMVLQAA GEFEAAKRYI LYRAERARER
     ERRPVPDHVR RAFDEARVYF PTALQQFQFF DKYSRFNYEL GRRETWIETV DRAVDYLYEL
     AGDRLPRETY ERIRRNILEM RSMPSMRLLA MAGPAARRNA VAIYNCSYQP VESIDSFVEA
     LIISMAGCGV GFSVESRYVE NFPRIKRQTG KPPVTFVVED SAEGWADALR YGLETWFEGG
     DVHFDLSHLR PAGAPLRTKG GRASGPEPFR AMLDFVRNRI FARQGSFLRP IDAHDIMCAV
     GNAAVSGGVR RTAMISLFDY DDDEMRLAKA GDFERENSQR WNANNSAVWP RGGLTQREFI
     RHFMEMIESQ RGEPGIFNRE AANLMKPARR KEADFGTNPC GEIVLRPWQF CNLSAAVARV
     DDTFETLRDK VEVATIIGTI QSLATHFPGL RPMWKQNCEE ERLLGVDITG QMDSPVAQDA
     QVKRRLKEIA IEVNRQTALS LGINPSAAIT CVKPSGNSSQ LLDCSSGLHA RWAPYYIRNV
     RVSAHSPLFK VLRDAGVPMD PENGQTREDA TTWVIHFPVK SPDGAITRNQ RSAIEQCEYW
     LQNKLYWTEH NPSCTVTYKP DEVIDLMKWV WDHRDMIGGL TFLPSFDAQY AQMPYVEITK
     EEYERLAAEF PEIDFSKIWR YEEEDLTTAA QELACMAGVC EVEVPPSA
//