ID C5A3W2_THEGJ Unreviewed; 911 AA.
AC C5A3W2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN Name=nrdA {ECO:0000313|EMBL:ACS32924.1};
GN OrderedLocusNames=TGAM_0422 {ECO:0000313|EMBL:ACS32924.1};
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117 {ECO:0000313|EMBL:ACS32924.1, ECO:0000313|Proteomes:UP000001488};
RN [1] {ECO:0000313|EMBL:ACS32924.1, ECO:0000313|Proteomes:UP000001488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3
RC {ECO:0000313|Proteomes:UP000001488};
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
CC -!- FUNCTION: Catalyzes the reduction of ribonucleotides to
CC deoxyribonucleotides. May function to provide a pool of
CC deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC and/or for immediate growth after restoration of oxygen.
CC {ECO:0000256|RuleBase:RU364064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922,
CC ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
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DR EMBL; CP001398; ACS32924.1; -; Genomic_DNA.
DR RefSeq; WP_015858042.1; NC_012804.1.
DR AlphaFoldDB; C5A3W2; -.
DR STRING; 593117.TGAM_0422; -.
DR PaxDb; 593117-TGAM_0422; -.
DR GeneID; 7987969; -.
DR KEGG; tga:TGAM_0422; -.
DR PATRIC; fig|593117.10.peg.418; -.
DR eggNOG; arCOG04276; Archaea.
DR HOGENOM; CLU_000404_2_3_2; -.
DR OrthoDB; 6188at2157; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001488; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR008926; RNR_R1-su_N.
DR NCBIfam; TIGR02504; NrdJ_Z; 1.
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; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 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};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 4..96
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 911 AA; 103851 MW; F275B612986C271E CRC64;
MAVEKVMKRD GRIVPFDRER IRWAIKRAML EVGVHDDKLL NRVVRRVVRR INELYDGQVP
HIENIQDIVE LELMRAGLFE VAKAYILYRK KKAEIREEKK KILNKDRLDE IDKRFSLNAL
RVLASRYLIR NEKGEIIESP RELFERVATL AVIPDLLYDE RVYDKNGKHE QDLSRVKYYL
EHFEEFDGRY SIGRFKLNKY HFERLVNLYR ELAEKGRMKV SIDEFLGMLE NGAFDDYESE
VEEYFRLMTG QVFMPNTPAL INSGRPLGML SACFVVPIED DMESIMKAAH DVAMIQKSGG
GTGLNFSKLR PEGDFVGSTA GAASGPVSFM HLIDAVSDVI KQGGVRRGAN MGILEVWHPD
IEKFIHAKEK NIGTNVLSNF NISVGIWEDF WEALRDGKRY PLVNPRTGEK VKEIDPKSLF
EELAFMAWSK ADPGVIFFDV INRRNVLEPA KGGPIRATNP CGEEPLYEYE SCNLASINLA
KFVKYDDEGK PYFDWDEYAY VIQKVAKYLD NAIDVNRFPL PEIDYNTKLT RRIGVGMMGL
ADALFKLGIP YNSEEGFAFM RKATEYLTFY AYKYSVEAAK KRGTFPLYEK SRYKDGELPV
EGFYHREIWN LPWDELVEEI KKHGVRNGMV TTCPPTGSVS MIADTSSGIE PIFALVYKKS
VTVGEFYYVD PVFEAELKKR GLWSDEILKK ISDNYGSVQG LEEIPEDMQR VFVTSMDVHW
LDHILAQANI QLWLTDSASK TINMPNDATV EDVKAAYLLA YKLGCKGITV YRDGSLSVQV
YSVEGEKRKR VPAKPSRYAV EKLKAVVEAE PWLAKFINVE AILNGTNGKG KAALPSGLTF
SVAHITPAKP PVREHPHHAE KPEIPEEKIK ELLGVAYCPV CYERDGELVE LRMESGCATC
PRCGWSKCVI S
//
