ID F2L4G2_THEU7 Unreviewed; 877 AA.
AC F2L4G2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN OrderedLocusNames=TUZN_1935 {ECO:0000313|EMBL:AEA13394.1};
OS Thermoproteus uzoniensis (strain 768-20).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=999630 {ECO:0000313|EMBL:AEA13394.1, ECO:0000313|Proteomes:UP000008138};
RN [1] {ECO:0000313|EMBL:AEA13394.1, ECO:0000313|Proteomes:UP000008138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=768-20 {ECO:0000313|EMBL:AEA13394.1,
RC ECO:0000313|Proteomes:UP000008138};
RX PubMed=21478349; DOI=10.1128/JB.00409-11;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL J. Bacteriol. 193:3156-3157(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=768-20;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002590; AEA13394.1; -; Genomic_DNA.
DR AlphaFoldDB; F2L4G2; -.
DR STRING; 999630.TUZN_1935; -.
DR KEGG; tuz:TUZN_1935; -.
DR eggNOG; arCOG03714; Archaea.
DR eggNOG; arCOG04276; Archaea.
DR HOGENOM; CLU_000404_2_3_2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008138; 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}.
FT DOMAIN 30..115
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 877 AA; 97648 MW; 7811B3C3722CC346 CRC64;
MGWAKVSFNS TPIILNIRDY IWKLGDDMAV KVIKASGAKE DFSEEKLRIS LVRAAADVGV
SVDGEVKIRP TSDITSAELS DLVELELLRK AIDKPELAEA AKSHLLGRIY KEALGKDFLR
DKSKYGERVF ASVERLVSAG LLKQEALSAL RWVELKPEFD RSLSYNALRL FTNGNYALRG
PDFKIAETPA AAAARVATAV AGSPEAARLY YDAITSLRIV PASPFWFNAW TKKEMFASCF
TLEVEDCLSS LTHPGRYCIY DALAYSGIIQ QLGGGVGYDF SLLRPEGDVV RGSVGVASGP
ISFMKLFDAN VDVIKQGGKR RGAQMGTLHV WHPDIRKFIK AKTGELKDAH LQNFNISVFV
DDTFMEKALG VDQNPKYPLI NPRVFYDKTG QKAVEHVDVY KEAEVPRDAI WGEVDASQLF
REISNSAWDS GDPGLIFKAN LNASNPLLGE EIEVAGYRFT YIWRSVNPCA ETVQNPFEVC
NLTHINLVKF IKDNCAGSSF EEKLACIDWE GLAQAARLGT RFLDSAIDRS RTGIEIVDEM
NSATRKNGLG IMGFAELLIK LGIPYASWEA VELINRIMGW IYVNALDASA DLAREKGPFK
YFEKSIYARG ELPALKFQDF VWSRWERVKH VYPPELRDAG DRLREITERT RQWLLPYIEK
LKEKVKGGVR NSVVLSIAPT GRTSILAGTT SGIEPVFALA FLRNVTVGTL VEYYEPGIEY
LKARGLWTPA VRKAVEETGM LRDAPVPEDV KHLLATAMEI GWLWHVLMQA SAQQWVDQGI
SKTINMPANA PSDDVYWAFA LAWALGVKGI TVYRDKSKSV QVIYTGLKQE IKKKLAETKI
TVRPISLETS IDEAANEVKL KALEEGKDPY CKTGECS
//
