ID V4LUU1_9CREN Unreviewed; 766 AA.
AC V4LUU1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=MGAcid_06450 {ECO:0000313|EMBL:ESQ22826.1};
OS uncultured Acidilobus sp. MG.
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus; environmental samples.
OX NCBI_TaxID=1410573 {ECO:0000313|EMBL:ESQ22826.1, ECO:0000313|Proteomes:UP000017902};
RN [1] {ECO:0000313|EMBL:ESQ22826.1, ECO:0000313|Proteomes:UP000017902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Rusch D.B., Tringe S.G., Bailey C., Jennings R.M., Inskeep W.P.;
RT "Predominant Acidilobus-like populations from geothermal environments of
RT Yellowstone National Park exhibit similar metabolic potential in different
RT hypoxic microbial communities.";
RL Submitted (OCT-2013) 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:ESQ22826.1}.
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DR EMBL; AYMA01000002; ESQ22826.1; -; Genomic_DNA.
DR AlphaFoldDB; V4LUU1; -.
DR STRING; 1410573.MGAcid_06450; -.
DR PATRIC; fig|1410573.3.peg.603; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000017902; 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: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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {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}.
FT DOMAIN 105..176
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 181..703
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 766 AA; 85510 MW; 06FF4D303B19DA39 CRC64;
MKIKLVRVQR VPGLTRSDVI AWAKEAARLA GLEPSKIEFE LLKLGARSPE ETYRKALEAF
ASWGLLDPTW EEAARRLVLA RIYHERGLQP PAKLEGIEAW ASWVGLNLLY ERYLIKRGEV
VVESPNEMLE RVASFVAGAE LGLGGRADEA KQEFYELMST GHFIPNSPTL MNSGTKYHQL
AACFVIPVDD DLDSIFNALN SAAWVFKTGA GAGFDFTPLR ARGTRLSSGG VASGPVSFMR
LFDQVADVIK EGGRRRAAMM GVLHDVHADL LSFIESKLGG GLENFNISVG VHDAFIMAAL
EGREWNLYDP YECPQLVGLL SSDLPDLWRK CVPKVTVNAA EVLDRAAKAA WEVGDPGLVF
IDTINEHNPT PRLGRIRTTN PCGETPLLSW EACNLGSINL SKYVVNGGID WDLLEHDVRV
AVRFLDDVIE ASWYPRPEIE KAVKRTRKIG LGVMGWADML AQLRVPYDSD SALLLADRLM
EFIAYVARGE SDRLASERGP YPEFPGSIHR EGRFNFEPQV SSSQIYDESK ASEDVLRIVE
SRPSLDWDRV RSEMREGTRN ATVTTIAPTG SISIIANASS SIEPFYSLIY VRQSSLFSWI
EVNRFLKEWL IETNNLRPER IKEIIMHGGS VRGLDWVDKE VQDVLGTALD IDWRWHVRMQ
AVFQRWVDNA VSKTVNLRHE VTPEDVKNVF LEAWRLKCKG VTVFRDRSKG VQVMQVPADL
DQLIREPPAM GVKVKAKMVP GVISAGNARI VTVSEEYAGG CPTCDL
//
