ID A0A0P6YPE6_9CHLR Unreviewed; 856 AA.
AC A0A0P6YPE6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=SE15_04210 {ECO:0000313|EMBL:KPL84793.1};
OS Thermanaerothrix daxensis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Thermanaerothrix.
OX NCBI_TaxID=869279 {ECO:0000313|EMBL:KPL84793.1, ECO:0000313|Proteomes:UP000050544};
RN [1] {ECO:0000313|EMBL:KPL84793.1, ECO:0000313|Proteomes:UP000050544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GNS-1 {ECO:0000313|EMBL:KPL84793.1,
RC ECO:0000313|Proteomes:UP000050544};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Whole genome sequence of Thermanaerothrix daxensis DSM 23592.";
RL Submitted (JUL-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPL84793.1}.
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DR EMBL; LGKO01000002; KPL84793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P6YPE6; -.
DR STRING; 869279.SE15_04210; -.
DR PATRIC; fig|869279.4.peg.852; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000050544; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IPR013346; NrdE_NrdA_C.
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; TIGR02506; NrdE_NrdA; 1.
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.
PE 3: Inferred from homology;
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|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064};
KW Reference proteome {ECO:0000313|Proteomes:UP000050544}.
FT DOMAIN 22..100
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 103..635
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 856 AA; 94845 MW; 61F96C582F5CEC3A CRC64;
MSNKNGLLPT PPLPGDLPSV HLTENARQVL IRRYVRRGED GQPVESVEEM FWRVAYHIAK
VEENWGGDVM QSAREFYLLL TSKKFFPNSP TFTGAGTPLG QLAACFVLPI SDDMGREPDG
IFQTLRDAAL IQQTGGGNGF SFSRLRPKGT LVKSSAGQAT GPVGFLRVYD HAFGEIAQGG
TRRGANMGVL RVDHPDIEDF ITCKTDENAI TNFNISVGIT DAFMRAVEND EEWELRFPDV
RSPRYREVKG TLEQLEAAGV PIVTYRRVRA RDLFNKIVKQ AHHNGEPGVL FLDTANRSNP
VPHLYPLEAT NPCGEQWLGP YENCCLGSIN LNEHCGPNGT VDWETLRQSV ITATRFLDDV
VEANAYVPAV PQLKEAAHRA RRIGLGIMGL ADLMYHVGVR YGSEEGQEFA AQVMEFIRFH
AMKASIELAR QRGPFPAIKG SIYDPENLTW TPPRPLMPYQ RDWGRPPLDW DEVVEGIRLY
GIRNAAQTTI APTGTIATVA GCEGYGCEPV FALAYIRHVN DNGKDLQLTY ASPRFEEALR
EAGIPEEKRR EIFERVLREG TCQHIPDVPE HIRNVFVVAS DITAEEHVRM QATLQAFVDN
SISKTINFPE HATEEDVATA YMLAWKLGCK GLTVYVTGSR EKVVLETLAT AEKKKQAEEA
PRPEVPQQLP IWHDLKKPRP RYLPGFTYSI QTPLGKAFIT INENGEAQPF EVFVNTAKAG
SDTAAVSEAI GRLLSYILRL ASPIEPARRL REAADQLLGI GGGRSLGFGP NRVRSLPDGV
GQILDEYLRQ REERLQSQAG GGMPSPAPAP APEPEYLTFK NQPLLEFGDL CPECGQAAVV
NEEGCRKCYA CGYSEC
//
