ID Q3YRQ4_EHRCJ Unreviewed; 622 AA.
AC Q3YRQ4;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN OrderedLocusNames=Ecaj_0566 {ECO:0000313|EMBL:AAZ68601.1};
OS Ehrlichia canis (strain Jake).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484 {ECO:0000313|EMBL:AAZ68601.1, ECO:0000313|Proteomes:UP000000435};
RN [1] {ECO:0000313|Proteomes:UP000000435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake {ECO:0000313|Proteomes:UP000000435};
RX PubMed=16707693; DOI=10.1128/JB.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(2006).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; CP000107; AAZ68601.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YRQ4; -.
DR STRING; 269484.Ecaj_0566; -.
DR KEGG; ecn:Ecaj_0566; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_7_0_5; -.
DR InParanoid; Q3YRQ4; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000435; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
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 Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 41..105
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 109..429
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 440..583
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 622 AA; 71191 MW; 76B2879A6EDC3E05 CRC64;
MFYIVNTYNI YAFLQYVVLN DEKMVEIMRK VIVDYGRDNN LTSFGKAVLS DRYLLENEDY
QQLFVRISEY YSDNPEHAQR LYDYMSQLWF MPATPILSNG GTNRGLPISC FLNETEDSLR
GIVNLWNENV WLASKGGGIG SYWGNLRSIG EKVRGSGKTS GIIPFIVVQN ALTLAISQGS
LRRGSSAVYL PVWHPEIEEF LDLRKPTGGD PNRKALNIHH GVVLSDKFMK CVENDEPWDL
ISPKDQSVIF TVKARDIWIK ILTTRVETGE PYILFIDQVE QNKPEIYKKL NLNIKMSNLC
TEITLTTGYD HLNKSRTAIC CLASLNLEYY EKWKDNSLFI EDVMRFLDNV LTDFIEKAPN
DMERAKYSAM RERSIGVGVM GFHSFLQSKM IPFESVAATI WNKKIFSHIK RHADAASYNI
AMEKGSCPDA QDAGVIERFV NKLSIAPTAS ISIIAGNTSP GIEPYAANVF THKTLTGSFI
VRNKFLQKLL IVKGKDNEQV WSSISTNEGS VQHLDFLTEE EKLIFKTAYE LDQRWIIEHT
SDRSKYICQA QSVNIFLPAN VHKRYLHKIH FLAWKKGLKS LYYCRSKSIQ RADKVSHGAL
EKSVEQYKQI TNFDYNECLS CQ
//
