ID A0A3S2V5U8_9SPHN Unreviewed; 647 AA.
AC A0A3S2V5U8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=EOE18_12675 {ECO:0000313|EMBL:RVU04349.1};
OS Novosphingobium umbonatum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1908524 {ECO:0000313|EMBL:RVU04349.1, ECO:0000313|Proteomes:UP000282837};
RN [1] {ECO:0000313|EMBL:RVU04349.1, ECO:0000313|Proteomes:UP000282837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSY-9 {ECO:0000313|EMBL:RVU04349.1,
RC ECO:0000313|Proteomes:UP000282837};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVU04349.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SACO01000009; RVU04349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2V5U8; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000282837; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000282837}.
FT DOMAIN 65..130
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 134..453
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 462..608
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 71919 MW; 197689F1089AC54A CRC64;
MAQTDQTKEA GQRPAMPMND KSDTALADLL VAATVTAAPE APVSDSKKIN PRRFKIVTDP
ARDALLTDFG KETLDDRYLL PDETYQDLFA RVADAYADDQ AHAQRLYDYI SRLWFMPATP
VLSNGGTGRG LPISCYLNTV EDSLEGIVNT WNENVWLASR GGGIGTYWGK VRGIGEAVGL
NGKTSGIIPF VRVMDSLTLA ISQGSLRRGS AAVYLDVSHP EIEEFLEIRK TSGDFNRKAL
NLHHGVLITD EFMQAVRDGR EFELKSPKDG SVRGKVDARS LFQKLVEVRL ATGEPYLVFS
DTVNRMMPQH HRDLGLKVYT SNLCSEITLP TGRDHLGNDR TAVCCLSSLN LETWDQWNGD
KRFIEDVLRF LDNVLQDYID RAPNEMSRAK YAAMRERSVG MGVMGFHSFL QLKGIPFESA
MAKAWNLKMF KHVASKADEA SILLAQERGA CPDAAEMGVM QRFSCKMAIA PTASISIICG
GTSACIEPIP ANIYTHKTLS GSFVIKNPYL KKLLAEKSKD STNVWNSILE HGGSVQHLDF
LSPDEKATYK TSFEIDQRWL LEFAADRTPF IDQAQSLNLY IPADVDKWDL MMLHFQAWEK
GIKSLYYLRS KSIQRAGFAG GVEADNTAVA PKIELATTDY EECLACQ
//
