NDRZ_THEAC
ID NDRZ_THEAC Reviewed; 768 AA.
AC Q9HI70; P74911;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Vitamin B12-dependent ribonucleoside-diphosphate reductase;
DE Short=B12-dependent RNR;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN OrderedLocusNames=Ta1475;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10; 71-92 AND
RP 140-150, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=8990160; DOI=10.1073/pnas.94.1.53;
RA Tauer A., Benner S.A.;
RT "The B12-dependent ribonucleotide reductase from the archaebacterium
RT Thermoplasma acidophila: an evolutionary solution to the ribonucleotide
RT reductase conundrum.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:53-58(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000269|PubMed:8990160}.
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:0000269|PubMed:8990160};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000269|PubMed:8990160};
CC Note=5'-deoxyadenosylcobalamine (coenzyme B12).
CC {ECO:0000269|PubMed:8990160};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=64 uM for ADP (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:8990160};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8990160}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18239.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAC12593.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U73619; AAB18239.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL445067; CAC12593.1; ALT_INIT; Genomic_DNA.
DR PIR; T37459; T37459.
DR RefSeq; WP_048162175.1; NC_002578.1.
DR AlphaFoldDB; Q9HI70; -.
DR SMR; Q9HI70; -.
DR STRING; 273075.Ta1475; -.
DR EnsemblBacteria; CAC12593; CAC12593; CAC12593.
DR GeneID; 1456927; -.
DR KEGG; tac:Ta1475; -.
DR eggNOG; arCOG04276; Archaea.
DR HOGENOM; CLU_000404_2_3_2; -.
DR OrthoDB; 4783at2157; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:UniProtKB-UniPathway.
DR CDD; cd02888; RNR_II_dimer; 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 Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02504; NrdJ_Z; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cobalamin; Cobalt; Deoxyribonucleotide synthesis;
KW Direct protein sequencing; Disulfide bond; DNA synthesis;
KW Nucleotide-binding; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8990160"
FT CHAIN 2..768
FT /note="Vitamin B12-dependent ribonucleoside-diphosphate
FT reductase"
FT /id="PRO_0000428781"
FT DOMAIN 3..97
FT /note="ATP-cone"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT ACT_SITE 432
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 434
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 436
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249..250
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 432..436
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 579..583
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 250..445
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 552
FT /note="G -> A (in Ref. 1; AAB18239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 768 AA; 86666 MW; AC77E4E6A5193FB2 CRC64;
MIKEVVKRDG TVVPFEKNKI TMAIYKAMLS VKNGTMKDAE QLADKVVARL KDKERPSVEE
IQDVVEDVLM TSKIDGKTFT DVAKSYILYR EKRRAIREEK ELMGVKDDLK LTLNAVKVLE
ARYLLKDEDG KIIETPRQMF RRVASHIGIV EALYDYIKYK KTGKVPENAE IIGKVSPTQE
EVLRRAFGYM KEDGIIEGTF EEFMDFIQTK GTSAGHYINR FEEVMSSLDF VPNSPTLMNA
GTKLGQLSAC FVLPVGDSIE DIFETLKNTA LIHKSGGGTG FSFSRLRPKD DIVGSTKGVA
SGPVSFMKIF DVTTDVIKQG GKRRGANMGI LNYNHPDIME FILSKDSENK VLSNFNISVG
VTDDFFDKLD NDDYVDLVNP RTKKIMKRIK AREIWDAIID QAWKTADPGL IFLDEINRKN
PVKNVGDIES TNPCGEQPLL PYESCNLGSI NLSKYVVDGK KIDFDRLRET VWTATRFLDD
VIDANKFPVE QIKKVTRMTR KIGLGVMGFA DMLIKLEIPY NSWEALEIGE KVMSFINDES
HKASQALAEE RGVFPAWYGS EWEKEGIKMR NSTTTTIAPT GTISIIAGCS SSIEPIFALA
FVRHVLNGQE LLEVNPLFEE KTRELGIYSE ELMRQVAETG NLENVKINEE VKKIFVTAHE
IDPQWHVLMQ ATFQRYCDSG VSKTINMRSD ATREDIARAY RMAKDLHCKG ITVYRDKSKT
VQVLTAGTAE TKKPEEKEVI ELVTKMPDKY LKIDSTFDPA CPTGKCDK
