ID A0A1F6WX53_9BACT Unreviewed; 857 AA.
AC A0A1F6WX53;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-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=A3A05_01775 {ECO:0000313|EMBL:OGI86384.1};
OS Candidatus Nomurabacteria bacterium RIFCSPLOWO2_01_FULL_41_12.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801774 {ECO:0000313|EMBL:OGI86384.1, ECO:0000313|Proteomes:UP000176187};
RN [1] {ECO:0000313|EMBL:OGI86384.1, ECO:0000313|Proteomes:UP000176187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGI86384.1}.
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DR EMBL; MFUY01000007; OGI86384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6WX53; -.
DR STRING; 1801774.A3A05_01775; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000176187; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
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; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 3..94
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 857 AA; 97271 MW; 199FB48ED30DF28E CRC64;
MTITITKRDG TKVPFNADRI NKSIERACYG IADPISKVIQ IATETQLTLY DGITTEEMDA
ATINAALQNT QYGIEFDKIA TRLLLKVIYK KVIGDYDNDE SKSTSPEEFA KLHSAHFKKY
ILNAVERGLL DSKMARAFDL EDLAASLKIE NDELYKYSGL STMQNRYLMK NELQAPLETP
QYFWMRVAMG MSLNEKNPTE WAKRFYEKMS KLEYLSAGSS NIGAGTPHPK LSNCYLMEMH
DDMEHIGKTV SDVLLLSKAT GGIGLSVTKL RAEGSVLKSN NTVSSGPVPF MHIIDSAVRA
VQRGGKKKGA LCFYMENWHL NFQDFLDLKQ NNGDDYRRTR TANTAVFISD EFMKRVLEGA
DWYLFDPKEV KDLPELYGKE FSTRYNEYVK MAKAGKIKMY NVIPARQQYK NILISLETTS
HPWLTWKDSI NIRALNNNTG TIHCSNLCTE VTLPTDKDNV AVCNLVSINM ARHIVNSQVD
WHRLEESVRL ATRQLDNLVD INERPIPEAV RADCENRAVG LGLMGFADSI EQLGYSYEDS
DAADFADQVF EFVSYMSIDE SANLAEERGS YKNFKGSGWS KGEVPIDTLK KLEMDRDREL
TVKKESAKLL PLLDWERARS KVKKGMRNAT LLAIAPNANI GLVAGTSPGI DPRFTQMFSR
NKISGKYLEV NPNMMEALKK ENLWEKTREA ILENHGDIEM IPEIPDHIKK IYKTSFSISP
YAYIEVAARA QKWVDMGISR NMYLEIRDIN EIMNIYTTAW DKGLKTTYYL HMKPRHTAEQ
STTVVNKAEV LGKRGFAVLR DKVVQQEIAK EITDAQEEVV IPEPSPIQMK EPVPAIKPPE
IEIVEDPQEK FLCESCQ
//
