ID Q3Z9K7_DEHM1 Unreviewed; 761 AA.
AC Q3Z9K7;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN Name=nrd-2 {ECO:0000313|EMBL:AAW40400.1};
GN OrderedLocusNames=DET0345 {ECO:0000313|EMBL:AAW40400.1};
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164 {ECO:0000313|EMBL:AAW40400.1, ECO:0000313|Proteomes:UP000008289};
RN [1] {ECO:0000313|EMBL:AAW40400.1, ECO:0000313|Proteomes:UP000008289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195
RC {ECO:0000313|Proteomes:UP000008289};
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., Deboy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
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; CP000027; AAW40400.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z9K7; -.
DR STRING; 243164.DET0345; -.
DR KEGG; det:DET0345; -.
DR eggNOG; COG0209; Bacteria.
DR eggNOG; COG1594; Bacteria.
DR HOGENOM; CLU_000404_2_0_0; -.
DR InParanoid; Q3Z9K7; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008289; 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: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; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR024434; TSCPD_dom.
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 Pfam; PF12637; TSCPD; 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}.
FT DOMAIN 21..102
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 105..573
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 640..707
FT /note="TSCPD"
FT /evidence="ECO:0000259|Pfam:PF12637"
SQ SEQUENCE 761 AA; 82977 MW; EAF472BA7206F35B CRC64;
MPVKVQVKSE IKADAKTEGL KLTDNAMCVL ERRYLKKDKQ GKPSETVEDM FRRVARTIAM
GELIYNPKAD VRSREDEFYN IMTRLEFLPN SPTLMNAGRE LGQLSACFVL PVDDSIESIF
DAVKHTAMIH KSGGGTGFSF SRLRPEQDRV GTTGGVASGP VSFMRAFDVA TDVIKQGGTR
RGANMAILSI DHPDIMKFIH AKDKAGVLTN FNLSVAITDK FMQAVKDGVD YDLLNPHNGE
VVSRLNATEV FNKIVHMAWK TGDPGIVFID RINAYNPTPQ LGRIESTNPC GEQPLLPYES
CNLGSINLSR MVTVSGGQAV VDYKKLSRVV KSAVRFLDNV IDVNKFPLPQ IEEMTKKSRK
IGLGVMGFAD MLLELGIPYN SENSIKLAEE IMCFVNEEAH KFSSELAVER GVFPAYRGSI
YEKSGRPMRN ASCTTIAPTG TLSIIAGCSS GIEPHFALCF TRNILDGTKM IEVNPYFERA
AKEGGYYSEE LIKSLAEGAH LDEADVPAEA KELFVTAHQI VPEWHVRIQA AFQKCTDNAV
SKTVNFSREA VEGDVAEVYK MAHDSNLKGI TIYRDGSRED QPMSTGKAEN KIETPAAVVN
PNLAPRKRSK VTQGITERVT TGCGYIYVTV NSDEHGICEV FSSLGKAGGC ASAQLESTCR
LISLALRSGM EVASVVKQLR GIRCPSIAWD DSKAVLSCAD AIASVLEKHV DGYTQPVAGS
AKTVSANALV RNIAGQCPEC GSILVYQEGC FICPGCGYTK C
//
