ID G4RL15_THETK Unreviewed; 845 AA.
AC G4RL15;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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:CCC82260.1};
GN OrderedLocusNames=TTX_1636 {ECO:0000313|EMBL:CCC82260.1};
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC82260.1, ECO:0000313|Proteomes:UP000002654};
RN [1] {ECO:0000313|EMBL:CCC82260.1, ECO:0000313|Proteomes:UP000002654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000313|Proteomes:UP000002654};
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
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; FN869859; CCC82260.1; -; Genomic_DNA.
DR RefSeq; WP_014127514.1; NC_016070.1.
DR AlphaFoldDB; G4RL15; -.
DR STRING; 768679.TTX_1636; -.
DR PaxDb; 768679-TTX_1636; -.
DR GeneID; 11262518; -.
DR KEGG; ttn:TTX_1636; -.
DR PATRIC; fig|768679.9.peg.1656; -.
DR eggNOG; arCOG04276; Archaea.
DR HOGENOM; CLU_000404_2_3_2; -.
DR OrthoDB; 6188at2157; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002654; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002654}.
FT DOMAIN 3..88
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 845 AA; 94383 MW; C3E81F1D519357FC CRC64;
MAVRVIKSSG HREEFSEDKL KSSLAKAARD VGVEVDGEVS ITPKGDVYSY ELSDIAELEL
LRRAIDDPKY AAVATSHLLG RVYKEALGKD FLKHKSGYGE RAVAKFEQLA SEGLIKGEAL
SLLRAFEPRP DFDRSLSYNA LRLFTNGNYA LRGGDFRLAE TPSMAAWRVA TAVARDTEMA
RRYYGAITSL KIVPASPFWF NAWTKKEMFA SCFTLEVEDC LSSLSHPNRF CIYDALAYSG
IIQQLGGGVG YDFSLLRPEG DVVRGSVGVA SGPISFMKLF DTNVEVIKQG GKRRGAQMGT
LHVWHPDVRK FIKAKTGELK DAHLQNFNIS VFADDSFMEK ALGLDKDPRY PLVNPRIYLE
KTGRKPVEEL RLSPPQEAVA GWADARELFR EIAEGAWDSG DPGVIYKDNL NASNPLLGVE
VEVAGYKFRY VWRSVNPCAE TVQNPFEVCN LTHINLAKFA RECTGKTLEE KLACIDWDGL
AEAARLGTRF LDEAIDRSRT GIGIIDEMNR ATRKNGLGIM GFAELLIKLG IPYASWEAVE
LINRIMAWIY VNALDESAEL ARERGPFKFF EESAYARGEI PVLKFQDYVW GKWERVRGAF
PPELREAGDR LREITMRTRE WLGPRLEALR EKVKGGVRNS VVLSIAPTGR TSILAGTTSG
VEPVFALAFI RNVTVGTLIE YYWPAVEWLR ARGLWTPQVR KTVEETGMLK DAPLPEEVKH
LFATAMEIGW LWHVLMQASA QQWVDQGISK TINMPANAPK EDVYWAFALA WALGVKGITV
YRDKSKSVQV IYTGLKQEIK KKLADTKIIV KPVALEASIE EAAEQAKLKA LEEGKDPYCK
TGECG
//
