ID A0A1Z9MR99_9RICK Unreviewed; 591 AA.
AC A0A1Z9MR99;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=CBD71_04815 {ECO:0000313|EMBL:OUW69804.1};
OS Rickettsiales bacterium TMED211.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX NCBI_TaxID=1986869 {ECO:0000313|EMBL:OUW69804.1, ECO:0000313|Proteomes:UP000195710};
RN [1] {ECO:0000313|EMBL:OUW69804.1, ECO:0000313|Proteomes:UP000195710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED211 {ECO:0000313|EMBL:OUW69804.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OUW69804.1}.
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DR EMBL; NHJI01000070; OUW69804.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000195710; Unassembled WGS sequence.
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 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; 3.
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 24..84
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 88..213
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 214..384
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 392..548
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 591 AA; 66376 MW; 5724986EA3C564D7 CRC64;
MWNNDWKKGT DYPEWGDTDV YKQTISGGYL LKNESPSEAY KRVCNTVARR LDRPELAEIF
YEYIWKGWLC LASPVLSNTG TDRGLPISCF GIDVADSIND IGKKNLEMML LAKHGGGVGI
GINQIRPAGS KITGNGTSDG VVPFCKIYDS TILATNQGSV RRGAASVNIN INHADFEEWL
EIREPKGDVN RQSLNLHQCA VVGDKFMRKL ESGDINARKK WSKLLQKRKA TGEPYILFKG
NTNKSNPEAY KQNALKVHMT NICSEIVLHT DESHSFVCCL SSLNLAKYEE WKDTNIIYDA
TWFLDGVLED FIQKAKGKIG FENSVRSAEK GRALGLGVLG WHTYLQEKGI PFEGLLSQYE
TRKIFSQIKI ESERASMDLA EAYGEPLWCV GQGLRNTHLR AIAPTVSNSK LSGNVSPGIE
PWAANVFTDQ SAKGTFIRKN PTLVRLLKKY KINTKKVWDK IMEDGGSVQD VKELDNIILE
NDIPAKDVFK TFKEINQLEI VNQAGLRQQY IDQSVSLNLA FPSEANPKWI NKVHFDAWKK
GIKTLYYMRT ESVLRGDIAA SAMDPNCVAC DGXKIIKGDQ LRPPFMQERW G
//
