ID D9Q2W9_ACIS3 Unreviewed; 756 AA.
AC D9Q2W9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN OrderedLocusNames=ASAC_1252 {ECO:0000313|EMBL:ADL19657.1};
OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS 345-15).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus.
OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL19657.1, ECO:0000313|Proteomes:UP000000346};
RN [1] {ECO:0000313|EMBL:ADL19657.1, ECO:0000313|Proteomes:UP000000346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC {ECO:0000313|Proteomes:UP000000346};
RX PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT a new order, Acidilobales, and suggests an important ecological role in
RT terrestrial acidic hot springs.";
RL Appl. Environ. Microbiol. 76:5652-5657(2010).
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; CP001742; ADL19657.1; -; Genomic_DNA.
DR RefSeq; WP_013267169.1; NC_014374.1.
DR AlphaFoldDB; D9Q2W9; -.
DR STRING; 666510.ASAC_1252; -.
DR GeneID; 9499507; -.
DR KEGG; asc:ASAC_1252; -.
DR eggNOG; arCOG04276; Archaea.
DR HOGENOM; CLU_000404_2_3_2; -.
DR InParanoid; D9Q2W9; -.
DR OrthoDB; 6188at2157; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000346; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000346}.
FT DOMAIN 95..166
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 171..693
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 756 AA; 84563 MW; 6BAEA5A00593F649 CRC64;
MRELTRTKVI AWAKQASRDA GLDPSQIEFE LLRLQASSPQ ELFTKALSTF ASWSLLDPRW
EEAARRLILY KIYEEKGSEA PGKLEGIESW ATWVGLNLLY ERYLVKRKGF VVETPNEALE
RVASFVAEAE LSLGGSLDAA RQEFYEIMSS GRFMPNSPTI MNSGTKYHQL AACFVIPLED
DMDSIFSALN TAAWVFKTGA GAGFDFTPLR GRGSPLSFGG TASGPVSFMK LFDEVADVIK
EGGRRRAAMM GVLHDVHVDL EDFINSKLSG GLENFNISVG VHDAFMMAAA SDSEWNLYDP
NECPQLVGLL SGDLPDLWRR CSPRRTVRAS SLLEEAARAA WETGDPGLVF LDTINQHNPT
PRLGRIRATN PCGETPLLSW EACNLGSLNL GRYVKDEGID WELLEHDIRI AVRFLDDVIE
TSWYPRPEIE AAVKRTRKIG LGVMGWADML AKLKIPYDSD SALYLADKLM EFIAYVARDE
SNRLSRERGP YPEFPGSIHK DGRFNFEPQV SSSQIYDESK VSDAVHSIVN SRPKLDWDRV
RSEMMEGTRN ATMTTIAPTG SISIIADASS SIEPFYSLIY IRQSSLFSWV ELNRFLRDWL
QESNNLNAEK IKDVIRHGGS VRGLSWVPSD VQAVLGTALD IDWRWHVRMQ AVFQRWVDNA
VSKTVNMRRD ATVDDVKGVF IEAWRLKCKG ITVFRDQSKG VQVMSVNQNI DALIREPPNL
RIRVKAKMVP GVINVEGSAL SAVSEEYAGG CPTCDL
//
